BcLTP, a novel lipid transfer protein in Brassica chinensis, may secrete and combine extracellular CaM
Abstract Lipid transfer proteins in plants are believed to be involved in many processes of cell physiology and development. In this work, a full-length cDNA encoding a novel lipid transfer protein, designated BcLTP was isolated from Brassica chinensis. At least two copies of BcLTP are present in wh...
Ausführliche Beschreibung
Autor*in: |
Wang, Chunming [verfasserIn] |
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Format: |
E-Artikel |
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Sprache: |
Englisch |
Erschienen: |
2007 |
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Schlagwörter: |
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Anmerkung: |
© Springer-Verlag 2007 |
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Übergeordnetes Werk: |
Enthalten in: Plant cell reports - Berlin : Springer, 1981, 27(2007), 1 vom: 22. Sept., Seite 159-169 |
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Übergeordnetes Werk: |
volume:27 ; year:2007 ; number:1 ; day:22 ; month:09 ; pages:159-169 |
Links: |
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DOI / URN: |
10.1007/s00299-007-0434-4 |
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Katalog-ID: |
SPR003893758 |
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100 | 1 | |a Wang, Chunming |e verfasserin |4 aut | |
245 | 1 | 0 | |a BcLTP, a novel lipid transfer protein in Brassica chinensis, may secrete and combine extracellular CaM |
264 | 1 | |c 2007 | |
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520 | |a Abstract Lipid transfer proteins in plants are believed to be involved in many processes of cell physiology and development. In this work, a full-length cDNA encoding a novel lipid transfer protein, designated BcLTP was isolated from Brassica chinensis. At least two copies of BcLTP are present in whole genome of B. chinensis, and its transcripts preferably accumulate in second-year organs, implying its role in reproductive growth stage. The 118 amino acid sequence deduced from a 354 bp open reading frame (ORF) shares common features with other members of plants LTPs family. A putative signal peptide at the N terminus was tested for secretion function by the yeast signal sequence trap (YSST) system, and further confirmed by vesicular and extracellular localization of YFP fusion protein. A highly conserved CaM binding site at C terminus was found and the binding properties with two representative CaM isoforms, one is convergent AtCaM2, one is divergent SCaM5, were determined by gel overlay. We found that convergent AtCaM2 prefer high concentration of $ Ca^{2+} $ for binding BcLTP, while SCaM5 does not depend on $ Ca^{2+ } $concentration too much for binding BcLTP. The lipid binding feature of BcLTP was demonstrated using florescence-marked 1-pyrenedodecanoic acid, which can be enhanced by AtCaM2 in $ Ca^{2+ } $dependent manner and by SCaM5 in either presence or absence of $ Ca^{2+} $. The collected data suggest that BcLTP may secrete and combine extracellular CaM isoforms, which in turn, facilitate lipid binding of BcLTP via $ Ca^{2+} $ mediated signaling. | ||
650 | 4 | |a Lipid transfer protein |7 (dpeaa)DE-He213 | |
650 | 4 | |a CaM isoforms |7 (dpeaa)DE-He213 | |
650 | 4 | |a Extracellular space |7 (dpeaa)DE-He213 | |
700 | 1 | |a Xie, Wanqin |4 aut | |
700 | 1 | |a Chi, Fang |4 aut | |
700 | 1 | |a Hu, Wenquan |4 aut | |
700 | 1 | |a Mao, Guohong |4 aut | |
700 | 1 | |a Sun, Daye |4 aut | |
700 | 1 | |a Li, Cuifeng |4 aut | |
700 | 1 | |a Sun, Ying |4 aut | |
773 | 0 | 8 | |i Enthalten in |t Plant cell reports |d Berlin : Springer, 1981 |g 27(2007), 1 vom: 22. Sept., Seite 159-169 |w (DE-627)254630367 |w (DE-600)1462082-0 |x 1432-203X |7 nnns |
773 | 1 | 8 | |g volume:27 |g year:2007 |g number:1 |g day:22 |g month:09 |g pages:159-169 |
856 | 4 | 0 | |u https://dx.doi.org/10.1007/s00299-007-0434-4 |z lizenzpflichtig |3 Volltext |
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912 | |a GBV_ILN_2031 | ||
912 | |a GBV_ILN_2034 | ||
912 | |a GBV_ILN_2037 | ||
912 | |a GBV_ILN_2038 | ||
912 | |a GBV_ILN_2039 | ||
912 | |a GBV_ILN_2044 | ||
912 | |a GBV_ILN_2048 | ||
912 | |a GBV_ILN_2049 | ||
912 | |a GBV_ILN_2050 | ||
912 | |a GBV_ILN_2055 | ||
912 | |a GBV_ILN_2057 | ||
912 | |a GBV_ILN_2059 | ||
912 | |a GBV_ILN_2061 | ||
912 | |a GBV_ILN_2064 | ||
912 | |a GBV_ILN_2065 | ||
912 | |a GBV_ILN_2068 | ||
912 | |a GBV_ILN_2070 | ||
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912 | |a GBV_ILN_2118 | ||
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912 | |a GBV_ILN_2122 | ||
912 | |a GBV_ILN_2129 | ||
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912 | |a GBV_ILN_2147 | ||
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2007 |
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10.1007/s00299-007-0434-4 doi (DE-627)SPR003893758 (SPR)s00299-007-0434-4-e DE-627 ger DE-627 rakwb eng Wang, Chunming verfasserin aut BcLTP, a novel lipid transfer protein in Brassica chinensis, may secrete and combine extracellular CaM 2007 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag 2007 Abstract Lipid transfer proteins in plants are believed to be involved in many processes of cell physiology and development. In this work, a full-length cDNA encoding a novel lipid transfer protein, designated BcLTP was isolated from Brassica chinensis. At least two copies of BcLTP are present in whole genome of B. chinensis, and its transcripts preferably accumulate in second-year organs, implying its role in reproductive growth stage. The 118 amino acid sequence deduced from a 354 bp open reading frame (ORF) shares common features with other members of plants LTPs family. A putative signal peptide at the N terminus was tested for secretion function by the yeast signal sequence trap (YSST) system, and further confirmed by vesicular and extracellular localization of YFP fusion protein. A highly conserved CaM binding site at C terminus was found and the binding properties with two representative CaM isoforms, one is convergent AtCaM2, one is divergent SCaM5, were determined by gel overlay. We found that convergent AtCaM2 prefer high concentration of $ Ca^{2+} $ for binding BcLTP, while SCaM5 does not depend on $ Ca^{2+ } $concentration too much for binding BcLTP. The lipid binding feature of BcLTP was demonstrated using florescence-marked 1-pyrenedodecanoic acid, which can be enhanced by AtCaM2 in $ Ca^{2+ } $dependent manner and by SCaM5 in either presence or absence of $ Ca^{2+} $. The collected data suggest that BcLTP may secrete and combine extracellular CaM isoforms, which in turn, facilitate lipid binding of BcLTP via $ Ca^{2+} $ mediated signaling. Lipid transfer protein (dpeaa)DE-He213 CaM isoforms (dpeaa)DE-He213 Extracellular space (dpeaa)DE-He213 Xie, Wanqin aut Chi, Fang aut Hu, Wenquan aut Mao, Guohong aut Sun, Daye aut Li, Cuifeng aut Sun, Ying aut Enthalten in Plant cell reports Berlin : Springer, 1981 27(2007), 1 vom: 22. Sept., Seite 159-169 (DE-627)254630367 (DE-600)1462082-0 1432-203X nnns volume:27 year:2007 number:1 day:22 month:09 pages:159-169 https://dx.doi.org/10.1007/s00299-007-0434-4 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_647 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 27 2007 1 22 09 159-169 |
spelling |
10.1007/s00299-007-0434-4 doi (DE-627)SPR003893758 (SPR)s00299-007-0434-4-e DE-627 ger DE-627 rakwb eng Wang, Chunming verfasserin aut BcLTP, a novel lipid transfer protein in Brassica chinensis, may secrete and combine extracellular CaM 2007 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag 2007 Abstract Lipid transfer proteins in plants are believed to be involved in many processes of cell physiology and development. In this work, a full-length cDNA encoding a novel lipid transfer protein, designated BcLTP was isolated from Brassica chinensis. At least two copies of BcLTP are present in whole genome of B. chinensis, and its transcripts preferably accumulate in second-year organs, implying its role in reproductive growth stage. The 118 amino acid sequence deduced from a 354 bp open reading frame (ORF) shares common features with other members of plants LTPs family. A putative signal peptide at the N terminus was tested for secretion function by the yeast signal sequence trap (YSST) system, and further confirmed by vesicular and extracellular localization of YFP fusion protein. A highly conserved CaM binding site at C terminus was found and the binding properties with two representative CaM isoforms, one is convergent AtCaM2, one is divergent SCaM5, were determined by gel overlay. We found that convergent AtCaM2 prefer high concentration of $ Ca^{2+} $ for binding BcLTP, while SCaM5 does not depend on $ Ca^{2+ } $concentration too much for binding BcLTP. The lipid binding feature of BcLTP was demonstrated using florescence-marked 1-pyrenedodecanoic acid, which can be enhanced by AtCaM2 in $ Ca^{2+ } $dependent manner and by SCaM5 in either presence or absence of $ Ca^{2+} $. The collected data suggest that BcLTP may secrete and combine extracellular CaM isoforms, which in turn, facilitate lipid binding of BcLTP via $ Ca^{2+} $ mediated signaling. Lipid transfer protein (dpeaa)DE-He213 CaM isoforms (dpeaa)DE-He213 Extracellular space (dpeaa)DE-He213 Xie, Wanqin aut Chi, Fang aut Hu, Wenquan aut Mao, Guohong aut Sun, Daye aut Li, Cuifeng aut Sun, Ying aut Enthalten in Plant cell reports Berlin : Springer, 1981 27(2007), 1 vom: 22. Sept., Seite 159-169 (DE-627)254630367 (DE-600)1462082-0 1432-203X nnns volume:27 year:2007 number:1 day:22 month:09 pages:159-169 https://dx.doi.org/10.1007/s00299-007-0434-4 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_647 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 27 2007 1 22 09 159-169 |
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10.1007/s00299-007-0434-4 doi (DE-627)SPR003893758 (SPR)s00299-007-0434-4-e DE-627 ger DE-627 rakwb eng Wang, Chunming verfasserin aut BcLTP, a novel lipid transfer protein in Brassica chinensis, may secrete and combine extracellular CaM 2007 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag 2007 Abstract Lipid transfer proteins in plants are believed to be involved in many processes of cell physiology and development. In this work, a full-length cDNA encoding a novel lipid transfer protein, designated BcLTP was isolated from Brassica chinensis. At least two copies of BcLTP are present in whole genome of B. chinensis, and its transcripts preferably accumulate in second-year organs, implying its role in reproductive growth stage. The 118 amino acid sequence deduced from a 354 bp open reading frame (ORF) shares common features with other members of plants LTPs family. A putative signal peptide at the N terminus was tested for secretion function by the yeast signal sequence trap (YSST) system, and further confirmed by vesicular and extracellular localization of YFP fusion protein. A highly conserved CaM binding site at C terminus was found and the binding properties with two representative CaM isoforms, one is convergent AtCaM2, one is divergent SCaM5, were determined by gel overlay. We found that convergent AtCaM2 prefer high concentration of $ Ca^{2+} $ for binding BcLTP, while SCaM5 does not depend on $ Ca^{2+ } $concentration too much for binding BcLTP. The lipid binding feature of BcLTP was demonstrated using florescence-marked 1-pyrenedodecanoic acid, which can be enhanced by AtCaM2 in $ Ca^{2+ } $dependent manner and by SCaM5 in either presence or absence of $ Ca^{2+} $. The collected data suggest that BcLTP may secrete and combine extracellular CaM isoforms, which in turn, facilitate lipid binding of BcLTP via $ Ca^{2+} $ mediated signaling. Lipid transfer protein (dpeaa)DE-He213 CaM isoforms (dpeaa)DE-He213 Extracellular space (dpeaa)DE-He213 Xie, Wanqin aut Chi, Fang aut Hu, Wenquan aut Mao, Guohong aut Sun, Daye aut Li, Cuifeng aut Sun, Ying aut Enthalten in Plant cell reports Berlin : Springer, 1981 27(2007), 1 vom: 22. Sept., Seite 159-169 (DE-627)254630367 (DE-600)1462082-0 1432-203X nnns volume:27 year:2007 number:1 day:22 month:09 pages:159-169 https://dx.doi.org/10.1007/s00299-007-0434-4 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_647 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 27 2007 1 22 09 159-169 |
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10.1007/s00299-007-0434-4 doi (DE-627)SPR003893758 (SPR)s00299-007-0434-4-e DE-627 ger DE-627 rakwb eng Wang, Chunming verfasserin aut BcLTP, a novel lipid transfer protein in Brassica chinensis, may secrete and combine extracellular CaM 2007 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag 2007 Abstract Lipid transfer proteins in plants are believed to be involved in many processes of cell physiology and development. In this work, a full-length cDNA encoding a novel lipid transfer protein, designated BcLTP was isolated from Brassica chinensis. At least two copies of BcLTP are present in whole genome of B. chinensis, and its transcripts preferably accumulate in second-year organs, implying its role in reproductive growth stage. The 118 amino acid sequence deduced from a 354 bp open reading frame (ORF) shares common features with other members of plants LTPs family. A putative signal peptide at the N terminus was tested for secretion function by the yeast signal sequence trap (YSST) system, and further confirmed by vesicular and extracellular localization of YFP fusion protein. A highly conserved CaM binding site at C terminus was found and the binding properties with two representative CaM isoforms, one is convergent AtCaM2, one is divergent SCaM5, were determined by gel overlay. We found that convergent AtCaM2 prefer high concentration of $ Ca^{2+} $ for binding BcLTP, while SCaM5 does not depend on $ Ca^{2+ } $concentration too much for binding BcLTP. The lipid binding feature of BcLTP was demonstrated using florescence-marked 1-pyrenedodecanoic acid, which can be enhanced by AtCaM2 in $ Ca^{2+ } $dependent manner and by SCaM5 in either presence or absence of $ Ca^{2+} $. The collected data suggest that BcLTP may secrete and combine extracellular CaM isoforms, which in turn, facilitate lipid binding of BcLTP via $ Ca^{2+} $ mediated signaling. Lipid transfer protein (dpeaa)DE-He213 CaM isoforms (dpeaa)DE-He213 Extracellular space (dpeaa)DE-He213 Xie, Wanqin aut Chi, Fang aut Hu, Wenquan aut Mao, Guohong aut Sun, Daye aut Li, Cuifeng aut Sun, Ying aut Enthalten in Plant cell reports Berlin : Springer, 1981 27(2007), 1 vom: 22. Sept., Seite 159-169 (DE-627)254630367 (DE-600)1462082-0 1432-203X nnns volume:27 year:2007 number:1 day:22 month:09 pages:159-169 https://dx.doi.org/10.1007/s00299-007-0434-4 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_647 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 27 2007 1 22 09 159-169 |
allfieldsSound |
10.1007/s00299-007-0434-4 doi (DE-627)SPR003893758 (SPR)s00299-007-0434-4-e DE-627 ger DE-627 rakwb eng Wang, Chunming verfasserin aut BcLTP, a novel lipid transfer protein in Brassica chinensis, may secrete and combine extracellular CaM 2007 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag 2007 Abstract Lipid transfer proteins in plants are believed to be involved in many processes of cell physiology and development. In this work, a full-length cDNA encoding a novel lipid transfer protein, designated BcLTP was isolated from Brassica chinensis. At least two copies of BcLTP are present in whole genome of B. chinensis, and its transcripts preferably accumulate in second-year organs, implying its role in reproductive growth stage. The 118 amino acid sequence deduced from a 354 bp open reading frame (ORF) shares common features with other members of plants LTPs family. A putative signal peptide at the N terminus was tested for secretion function by the yeast signal sequence trap (YSST) system, and further confirmed by vesicular and extracellular localization of YFP fusion protein. A highly conserved CaM binding site at C terminus was found and the binding properties with two representative CaM isoforms, one is convergent AtCaM2, one is divergent SCaM5, were determined by gel overlay. We found that convergent AtCaM2 prefer high concentration of $ Ca^{2+} $ for binding BcLTP, while SCaM5 does not depend on $ Ca^{2+ } $concentration too much for binding BcLTP. The lipid binding feature of BcLTP was demonstrated using florescence-marked 1-pyrenedodecanoic acid, which can be enhanced by AtCaM2 in $ Ca^{2+ } $dependent manner and by SCaM5 in either presence or absence of $ Ca^{2+} $. The collected data suggest that BcLTP may secrete and combine extracellular CaM isoforms, which in turn, facilitate lipid binding of BcLTP via $ Ca^{2+} $ mediated signaling. Lipid transfer protein (dpeaa)DE-He213 CaM isoforms (dpeaa)DE-He213 Extracellular space (dpeaa)DE-He213 Xie, Wanqin aut Chi, Fang aut Hu, Wenquan aut Mao, Guohong aut Sun, Daye aut Li, Cuifeng aut Sun, Ying aut Enthalten in Plant cell reports Berlin : Springer, 1981 27(2007), 1 vom: 22. Sept., Seite 159-169 (DE-627)254630367 (DE-600)1462082-0 1432-203X nnns volume:27 year:2007 number:1 day:22 month:09 pages:159-169 https://dx.doi.org/10.1007/s00299-007-0434-4 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_647 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 27 2007 1 22 09 159-169 |
language |
English |
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Enthalten in Plant cell reports 27(2007), 1 vom: 22. Sept., Seite 159-169 volume:27 year:2007 number:1 day:22 month:09 pages:159-169 |
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Enthalten in Plant cell reports 27(2007), 1 vom: 22. Sept., Seite 159-169 volume:27 year:2007 number:1 day:22 month:09 pages:159-169 |
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topic_facet |
Lipid transfer protein CaM isoforms Extracellular space |
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Plant cell reports |
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Wang, Chunming @@aut@@ Xie, Wanqin @@aut@@ Chi, Fang @@aut@@ Hu, Wenquan @@aut@@ Mao, Guohong @@aut@@ Sun, Daye @@aut@@ Li, Cuifeng @@aut@@ Sun, Ying @@aut@@ |
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2007-09-22T00:00:00Z |
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In this work, a full-length cDNA encoding a novel lipid transfer protein, designated BcLTP was isolated from Brassica chinensis. At least two copies of BcLTP are present in whole genome of B. chinensis, and its transcripts preferably accumulate in second-year organs, implying its role in reproductive growth stage. The 118 amino acid sequence deduced from a 354 bp open reading frame (ORF) shares common features with other members of plants LTPs family. A putative signal peptide at the N terminus was tested for secretion function by the yeast signal sequence trap (YSST) system, and further confirmed by vesicular and extracellular localization of YFP fusion protein. A highly conserved CaM binding site at C terminus was found and the binding properties with two representative CaM isoforms, one is convergent AtCaM2, one is divergent SCaM5, were determined by gel overlay. We found that convergent AtCaM2 prefer high concentration of $ Ca^{2+} $ for binding BcLTP, while SCaM5 does not depend on $ Ca^{2+ } $concentration too much for binding BcLTP. The lipid binding feature of BcLTP was demonstrated using florescence-marked 1-pyrenedodecanoic acid, which can be enhanced by AtCaM2 in $ Ca^{2+ } $dependent manner and by SCaM5 in either presence or absence of $ Ca^{2+} $. The collected data suggest that BcLTP may secrete and combine extracellular CaM isoforms, which in turn, facilitate lipid binding of BcLTP via $ Ca^{2+} $ mediated signaling.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Lipid transfer protein</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">CaM isoforms</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Extracellular space</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Xie, Wanqin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Chi, Fang</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Hu, Wenquan</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Mao, Guohong</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Sun, Daye</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Li, Cuifeng</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Sun, Ying</subfield><subfield code="4">aut</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">Plant cell reports</subfield><subfield code="d">Berlin : Springer, 1981</subfield><subfield code="g">27(2007), 1 vom: 22. 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|
author |
Wang, Chunming |
spellingShingle |
Wang, Chunming misc Lipid transfer protein misc CaM isoforms misc Extracellular space BcLTP, a novel lipid transfer protein in Brassica chinensis, may secrete and combine extracellular CaM |
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Wang, Chunming |
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electronic Article |
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aut aut aut aut aut aut aut aut |
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true |
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Not Illustrated |
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1432-203X |
topic_title |
BcLTP, a novel lipid transfer protein in Brassica chinensis, may secrete and combine extracellular CaM Lipid transfer protein (dpeaa)DE-He213 CaM isoforms (dpeaa)DE-He213 Extracellular space (dpeaa)DE-He213 |
topic |
misc Lipid transfer protein misc CaM isoforms misc Extracellular space |
topic_unstemmed |
misc Lipid transfer protein misc CaM isoforms misc Extracellular space |
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misc Lipid transfer protein misc CaM isoforms misc Extracellular space |
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Elektronische Aufsätze Aufsätze Elektronische Ressource |
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title |
BcLTP, a novel lipid transfer protein in Brassica chinensis, may secrete and combine extracellular CaM |
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BcLTP, a novel lipid transfer protein in Brassica chinensis, may secrete and combine extracellular CaM |
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Wang, Chunming |
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Plant cell reports |
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Plant cell reports |
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eng |
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2007 |
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Wang, Chunming Xie, Wanqin Chi, Fang Hu, Wenquan Mao, Guohong Sun, Daye Li, Cuifeng Sun, Ying |
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27 |
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Elektronische Aufsätze |
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Wang, Chunming |
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10.1007/s00299-007-0434-4 |
title_sort |
bcltp, a novel lipid transfer protein in brassica chinensis, may secrete and combine extracellular cam |
title_auth |
BcLTP, a novel lipid transfer protein in Brassica chinensis, may secrete and combine extracellular CaM |
abstract |
Abstract Lipid transfer proteins in plants are believed to be involved in many processes of cell physiology and development. In this work, a full-length cDNA encoding a novel lipid transfer protein, designated BcLTP was isolated from Brassica chinensis. At least two copies of BcLTP are present in whole genome of B. chinensis, and its transcripts preferably accumulate in second-year organs, implying its role in reproductive growth stage. The 118 amino acid sequence deduced from a 354 bp open reading frame (ORF) shares common features with other members of plants LTPs family. A putative signal peptide at the N terminus was tested for secretion function by the yeast signal sequence trap (YSST) system, and further confirmed by vesicular and extracellular localization of YFP fusion protein. A highly conserved CaM binding site at C terminus was found and the binding properties with two representative CaM isoforms, one is convergent AtCaM2, one is divergent SCaM5, were determined by gel overlay. We found that convergent AtCaM2 prefer high concentration of $ Ca^{2+} $ for binding BcLTP, while SCaM5 does not depend on $ Ca^{2+ } $concentration too much for binding BcLTP. The lipid binding feature of BcLTP was demonstrated using florescence-marked 1-pyrenedodecanoic acid, which can be enhanced by AtCaM2 in $ Ca^{2+ } $dependent manner and by SCaM5 in either presence or absence of $ Ca^{2+} $. The collected data suggest that BcLTP may secrete and combine extracellular CaM isoforms, which in turn, facilitate lipid binding of BcLTP via $ Ca^{2+} $ mediated signaling. © Springer-Verlag 2007 |
abstractGer |
Abstract Lipid transfer proteins in plants are believed to be involved in many processes of cell physiology and development. In this work, a full-length cDNA encoding a novel lipid transfer protein, designated BcLTP was isolated from Brassica chinensis. At least two copies of BcLTP are present in whole genome of B. chinensis, and its transcripts preferably accumulate in second-year organs, implying its role in reproductive growth stage. The 118 amino acid sequence deduced from a 354 bp open reading frame (ORF) shares common features with other members of plants LTPs family. A putative signal peptide at the N terminus was tested for secretion function by the yeast signal sequence trap (YSST) system, and further confirmed by vesicular and extracellular localization of YFP fusion protein. A highly conserved CaM binding site at C terminus was found and the binding properties with two representative CaM isoforms, one is convergent AtCaM2, one is divergent SCaM5, were determined by gel overlay. We found that convergent AtCaM2 prefer high concentration of $ Ca^{2+} $ for binding BcLTP, while SCaM5 does not depend on $ Ca^{2+ } $concentration too much for binding BcLTP. The lipid binding feature of BcLTP was demonstrated using florescence-marked 1-pyrenedodecanoic acid, which can be enhanced by AtCaM2 in $ Ca^{2+ } $dependent manner and by SCaM5 in either presence or absence of $ Ca^{2+} $. The collected data suggest that BcLTP may secrete and combine extracellular CaM isoforms, which in turn, facilitate lipid binding of BcLTP via $ Ca^{2+} $ mediated signaling. © Springer-Verlag 2007 |
abstract_unstemmed |
Abstract Lipid transfer proteins in plants are believed to be involved in many processes of cell physiology and development. In this work, a full-length cDNA encoding a novel lipid transfer protein, designated BcLTP was isolated from Brassica chinensis. At least two copies of BcLTP are present in whole genome of B. chinensis, and its transcripts preferably accumulate in second-year organs, implying its role in reproductive growth stage. The 118 amino acid sequence deduced from a 354 bp open reading frame (ORF) shares common features with other members of plants LTPs family. A putative signal peptide at the N terminus was tested for secretion function by the yeast signal sequence trap (YSST) system, and further confirmed by vesicular and extracellular localization of YFP fusion protein. A highly conserved CaM binding site at C terminus was found and the binding properties with two representative CaM isoforms, one is convergent AtCaM2, one is divergent SCaM5, were determined by gel overlay. We found that convergent AtCaM2 prefer high concentration of $ Ca^{2+} $ for binding BcLTP, while SCaM5 does not depend on $ Ca^{2+ } $concentration too much for binding BcLTP. The lipid binding feature of BcLTP was demonstrated using florescence-marked 1-pyrenedodecanoic acid, which can be enhanced by AtCaM2 in $ Ca^{2+ } $dependent manner and by SCaM5 in either presence or absence of $ Ca^{2+} $. The collected data suggest that BcLTP may secrete and combine extracellular CaM isoforms, which in turn, facilitate lipid binding of BcLTP via $ Ca^{2+} $ mediated signaling. © Springer-Verlag 2007 |
collection_details |
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container_issue |
1 |
title_short |
BcLTP, a novel lipid transfer protein in Brassica chinensis, may secrete and combine extracellular CaM |
url |
https://dx.doi.org/10.1007/s00299-007-0434-4 |
remote_bool |
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author2 |
Xie, Wanqin Chi, Fang Hu, Wenquan Mao, Guohong Sun, Daye Li, Cuifeng Sun, Ying |
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Xie, Wanqin Chi, Fang Hu, Wenquan Mao, Guohong Sun, Daye Li, Cuifeng Sun, Ying |
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doi_str |
10.1007/s00299-007-0434-4 |
up_date |
2024-07-03T22:21:18.251Z |
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score |
7.4020767 |