Signal peptide fragments of preprolactin and HIV‐1 p‐gp160 interact with calmodulin
Abstract Secretory proteins and most membrane proteins are synthesized with a signal sequence that is usually cleaved from the nascent polypeptide during transport into the lumen of the endoplasmic reticulum. Using site‐specific photo‐crosslinking we have followed the fate of the signal sequence of...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Martoglio, Bruno [verfasserIn] Graf, Roland [verfasserIn] Dobberstein, Bernhard [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1997 |
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| Schlagwörter: |
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| Anmerkung: |
© European Molecular Biology Organization 1997 |
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| Übergeordnetes Werk: |
Enthalten in: The EMBO Journal - Nature Publishing Group UK, 2023, 16(1997), 22 vom: 15. Nov., Seite 6636-6645 |
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| Übergeordnetes Werk: |
volume:16 ; year:1997 ; number:22 ; day:15 ; month:11 ; pages:6636-6645 |
| Links: |
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| DOI / URN: |
10.1093/emboj/16.22.6636 |
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| Katalog-ID: |
SPR05799904X |
|---|
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| 024 | 7 | |a 10.1093/emboj/16.22.6636 |2 doi | |
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| 041 | |a eng | ||
| 100 | 1 | |a Martoglio, Bruno |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Signal peptide fragments of preprolactin and HIV‐1 p‐gp160 interact with calmodulin |
| 264 | 1 | |c 1997 | |
| 336 | |a Text |b txt |2 rdacontent | ||
| 337 | |a Computermedien |b c |2 rdamedia | ||
| 338 | |a Online-Ressource |b cr |2 rdacarrier | ||
| 500 | |a © European Molecular Biology Organization 1997 | ||
| 520 | |a Abstract Secretory proteins and most membrane proteins are synthesized with a signal sequence that is usually cleaved from the nascent polypeptide during transport into the lumen of the endoplasmic reticulum. Using site‐specific photo‐crosslinking we have followed the fate of the signal sequence of preprolactin in a cell‐free system. This signal sequence has an unusually long hydrophilic n‐region containing several positively charged amino acid residues. We found that after cleavage by signal peptidase the signal sequence is in contact with lipids and subunits of the signal peptidase complex. The cleaved signal sequence is processed further and an N‐terminal fragment is released into the cytosol. This signal peptide fragment was found to interact efficiently with calmodulin. Similar to preprolactin, the signal sequence of the HIV‐1 envelope protein p‐gp160 has the characteristic feature for calmodulin binding in its n‐region. We found that a signal peptide fragment of p‐gp160 was released into the cytosol and interacts with calmodulin. Our results suggest that signal peptide fragments of some cellular and viral proteins can interact with cytosolic target molecules. The functional consequences of such interactions remain to be established. However, our data suggest that signal sequences may be functionally more versatile than anticipated up to now. | ||
| 650 | 4 | |a calmodulin |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a eukaryotic signal peptidase |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a HIV‐1 gp160 |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a prolactin secretion |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a signal sequence |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a Graf, Roland |e verfasserin |4 aut | |
| 700 | 1 | |a Dobberstein, Bernhard |e verfasserin |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t The EMBO Journal |d Nature Publishing Group UK, 2023 |g 16(1997), 22 vom: 15. Nov., Seite 6636-6645 |w (DE-627)266022529 |w (DE-600)1467419-1 |x 1460-2075 |7 nnns |
| 773 | 1 | 8 | |g volume:16 |g year:1997 |g number:22 |g day:15 |g month:11 |g pages:6636-6645 |
| 856 | 4 | 0 | |u https://dx.doi.org/10.1093/emboj/16.22.6636 |m X:SPRINGER |x Resolving-System |z lizenzpflichtig |3 Volltext |
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| 912 | |a GBV_ILN_2049 | ||
| 912 | |a GBV_ILN_2050 | ||
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| 912 | |a GBV_ILN_2056 | ||
| 912 | |a GBV_ILN_2057 | ||
| 912 | |a GBV_ILN_2059 | ||
| 912 | |a GBV_ILN_2061 | ||
| 912 | |a GBV_ILN_2064 | ||
| 912 | |a GBV_ILN_2068 | ||
| 912 | |a GBV_ILN_2088 | ||
| 912 | |a GBV_ILN_2093 | ||
| 912 | |a GBV_ILN_2106 | ||
| 912 | |a GBV_ILN_2108 | ||
| 912 | |a GBV_ILN_2110 | ||
| 912 | |a GBV_ILN_2111 | ||
| 912 | |a GBV_ILN_2113 | ||
| 912 | |a GBV_ILN_2118 | ||
| 912 | |a GBV_ILN_2119 | ||
| 912 | |a GBV_ILN_2122 | ||
| 912 | |a GBV_ILN_2129 | ||
| 912 | |a GBV_ILN_2143 | ||
| 912 | |a GBV_ILN_2144 | ||
| 912 | |a GBV_ILN_2147 | ||
| 912 | |a GBV_ILN_2148 | ||
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| 912 | |a GBV_ILN_2188 | ||
| 912 | |a GBV_ILN_2190 | ||
| 912 | |a GBV_ILN_2232 | ||
| 912 | |a GBV_ILN_2336 | ||
| 912 | |a GBV_ILN_2470 | ||
| 912 | |a GBV_ILN_2472 | ||
| 912 | |a GBV_ILN_2507 | ||
| 912 | |a GBV_ILN_2522 | ||
| 912 | |a GBV_ILN_2548 | ||
| 912 | |a GBV_ILN_4012 | ||
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| 912 | |a GBV_ILN_4126 | ||
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| 912 | |a GBV_ILN_4251 | ||
| 912 | |a GBV_ILN_4305 | ||
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| 912 | |a GBV_ILN_4323 | ||
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| 912 | |a GBV_ILN_4325 | ||
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| 912 | |a GBV_ILN_4333 | ||
| 912 | |a GBV_ILN_4334 | ||
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| 912 | |a GBV_ILN_4700 | ||
| 951 | |a AR | ||
| 952 | |d 16 |j 1997 |e 22 |b 15 |c 11 |h 6636-6645 | ||
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1997 |
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1997 |
| allfields |
10.1093/emboj/16.22.6636 doi (DE-627)SPR05799904X (SPR)16.22.6636-e DE-627 ger DE-627 rakwb eng Martoglio, Bruno verfasserin aut Signal peptide fragments of preprolactin and HIV‐1 p‐gp160 interact with calmodulin 1997 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 1997 Abstract Secretory proteins and most membrane proteins are synthesized with a signal sequence that is usually cleaved from the nascent polypeptide during transport into the lumen of the endoplasmic reticulum. Using site‐specific photo‐crosslinking we have followed the fate of the signal sequence of preprolactin in a cell‐free system. This signal sequence has an unusually long hydrophilic n‐region containing several positively charged amino acid residues. We found that after cleavage by signal peptidase the signal sequence is in contact with lipids and subunits of the signal peptidase complex. The cleaved signal sequence is processed further and an N‐terminal fragment is released into the cytosol. This signal peptide fragment was found to interact efficiently with calmodulin. Similar to preprolactin, the signal sequence of the HIV‐1 envelope protein p‐gp160 has the characteristic feature for calmodulin binding in its n‐region. We found that a signal peptide fragment of p‐gp160 was released into the cytosol and interacts with calmodulin. Our results suggest that signal peptide fragments of some cellular and viral proteins can interact with cytosolic target molecules. The functional consequences of such interactions remain to be established. However, our data suggest that signal sequences may be functionally more versatile than anticipated up to now. calmodulin (dpeaa)DE-He213 eukaryotic signal peptidase (dpeaa)DE-He213 HIV‐1 gp160 (dpeaa)DE-He213 prolactin secretion (dpeaa)DE-He213 signal sequence (dpeaa)DE-He213 Graf, Roland verfasserin aut Dobberstein, Bernhard verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 16(1997), 22 vom: 15. Nov., Seite 6636-6645 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:16 year:1997 number:22 day:15 month:11 pages:6636-6645 https://dx.doi.org/10.1093/emboj/16.22.6636 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER 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_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 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_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 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_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 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_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4318 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_4367 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 16 1997 22 15 11 6636-6645 |
| spelling |
10.1093/emboj/16.22.6636 doi (DE-627)SPR05799904X (SPR)16.22.6636-e DE-627 ger DE-627 rakwb eng Martoglio, Bruno verfasserin aut Signal peptide fragments of preprolactin and HIV‐1 p‐gp160 interact with calmodulin 1997 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 1997 Abstract Secretory proteins and most membrane proteins are synthesized with a signal sequence that is usually cleaved from the nascent polypeptide during transport into the lumen of the endoplasmic reticulum. Using site‐specific photo‐crosslinking we have followed the fate of the signal sequence of preprolactin in a cell‐free system. This signal sequence has an unusually long hydrophilic n‐region containing several positively charged amino acid residues. We found that after cleavage by signal peptidase the signal sequence is in contact with lipids and subunits of the signal peptidase complex. The cleaved signal sequence is processed further and an N‐terminal fragment is released into the cytosol. This signal peptide fragment was found to interact efficiently with calmodulin. Similar to preprolactin, the signal sequence of the HIV‐1 envelope protein p‐gp160 has the characteristic feature for calmodulin binding in its n‐region. We found that a signal peptide fragment of p‐gp160 was released into the cytosol and interacts with calmodulin. Our results suggest that signal peptide fragments of some cellular and viral proteins can interact with cytosolic target molecules. The functional consequences of such interactions remain to be established. However, our data suggest that signal sequences may be functionally more versatile than anticipated up to now. calmodulin (dpeaa)DE-He213 eukaryotic signal peptidase (dpeaa)DE-He213 HIV‐1 gp160 (dpeaa)DE-He213 prolactin secretion (dpeaa)DE-He213 signal sequence (dpeaa)DE-He213 Graf, Roland verfasserin aut Dobberstein, Bernhard verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 16(1997), 22 vom: 15. Nov., Seite 6636-6645 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:16 year:1997 number:22 day:15 month:11 pages:6636-6645 https://dx.doi.org/10.1093/emboj/16.22.6636 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER 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_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 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_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 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_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 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_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4318 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_4367 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 16 1997 22 15 11 6636-6645 |
| allfields_unstemmed |
10.1093/emboj/16.22.6636 doi (DE-627)SPR05799904X (SPR)16.22.6636-e DE-627 ger DE-627 rakwb eng Martoglio, Bruno verfasserin aut Signal peptide fragments of preprolactin and HIV‐1 p‐gp160 interact with calmodulin 1997 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 1997 Abstract Secretory proteins and most membrane proteins are synthesized with a signal sequence that is usually cleaved from the nascent polypeptide during transport into the lumen of the endoplasmic reticulum. Using site‐specific photo‐crosslinking we have followed the fate of the signal sequence of preprolactin in a cell‐free system. This signal sequence has an unusually long hydrophilic n‐region containing several positively charged amino acid residues. We found that after cleavage by signal peptidase the signal sequence is in contact with lipids and subunits of the signal peptidase complex. The cleaved signal sequence is processed further and an N‐terminal fragment is released into the cytosol. This signal peptide fragment was found to interact efficiently with calmodulin. Similar to preprolactin, the signal sequence of the HIV‐1 envelope protein p‐gp160 has the characteristic feature for calmodulin binding in its n‐region. We found that a signal peptide fragment of p‐gp160 was released into the cytosol and interacts with calmodulin. Our results suggest that signal peptide fragments of some cellular and viral proteins can interact with cytosolic target molecules. The functional consequences of such interactions remain to be established. However, our data suggest that signal sequences may be functionally more versatile than anticipated up to now. calmodulin (dpeaa)DE-He213 eukaryotic signal peptidase (dpeaa)DE-He213 HIV‐1 gp160 (dpeaa)DE-He213 prolactin secretion (dpeaa)DE-He213 signal sequence (dpeaa)DE-He213 Graf, Roland verfasserin aut Dobberstein, Bernhard verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 16(1997), 22 vom: 15. Nov., Seite 6636-6645 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:16 year:1997 number:22 day:15 month:11 pages:6636-6645 https://dx.doi.org/10.1093/emboj/16.22.6636 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER 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_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 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_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 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_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 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_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4318 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_4367 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 16 1997 22 15 11 6636-6645 |
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10.1093/emboj/16.22.6636 doi (DE-627)SPR05799904X (SPR)16.22.6636-e DE-627 ger DE-627 rakwb eng Martoglio, Bruno verfasserin aut Signal peptide fragments of preprolactin and HIV‐1 p‐gp160 interact with calmodulin 1997 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 1997 Abstract Secretory proteins and most membrane proteins are synthesized with a signal sequence that is usually cleaved from the nascent polypeptide during transport into the lumen of the endoplasmic reticulum. Using site‐specific photo‐crosslinking we have followed the fate of the signal sequence of preprolactin in a cell‐free system. This signal sequence has an unusually long hydrophilic n‐region containing several positively charged amino acid residues. We found that after cleavage by signal peptidase the signal sequence is in contact with lipids and subunits of the signal peptidase complex. The cleaved signal sequence is processed further and an N‐terminal fragment is released into the cytosol. This signal peptide fragment was found to interact efficiently with calmodulin. Similar to preprolactin, the signal sequence of the HIV‐1 envelope protein p‐gp160 has the characteristic feature for calmodulin binding in its n‐region. We found that a signal peptide fragment of p‐gp160 was released into the cytosol and interacts with calmodulin. Our results suggest that signal peptide fragments of some cellular and viral proteins can interact with cytosolic target molecules. The functional consequences of such interactions remain to be established. However, our data suggest that signal sequences may be functionally more versatile than anticipated up to now. calmodulin (dpeaa)DE-He213 eukaryotic signal peptidase (dpeaa)DE-He213 HIV‐1 gp160 (dpeaa)DE-He213 prolactin secretion (dpeaa)DE-He213 signal sequence (dpeaa)DE-He213 Graf, Roland verfasserin aut Dobberstein, Bernhard verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 16(1997), 22 vom: 15. Nov., Seite 6636-6645 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:16 year:1997 number:22 day:15 month:11 pages:6636-6645 https://dx.doi.org/10.1093/emboj/16.22.6636 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER 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_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 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_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 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_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 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_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4318 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_4367 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 16 1997 22 15 11 6636-6645 |
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10.1093/emboj/16.22.6636 doi (DE-627)SPR05799904X (SPR)16.22.6636-e DE-627 ger DE-627 rakwb eng Martoglio, Bruno verfasserin aut Signal peptide fragments of preprolactin and HIV‐1 p‐gp160 interact with calmodulin 1997 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 1997 Abstract Secretory proteins and most membrane proteins are synthesized with a signal sequence that is usually cleaved from the nascent polypeptide during transport into the lumen of the endoplasmic reticulum. Using site‐specific photo‐crosslinking we have followed the fate of the signal sequence of preprolactin in a cell‐free system. This signal sequence has an unusually long hydrophilic n‐region containing several positively charged amino acid residues. We found that after cleavage by signal peptidase the signal sequence is in contact with lipids and subunits of the signal peptidase complex. The cleaved signal sequence is processed further and an N‐terminal fragment is released into the cytosol. This signal peptide fragment was found to interact efficiently with calmodulin. Similar to preprolactin, the signal sequence of the HIV‐1 envelope protein p‐gp160 has the characteristic feature for calmodulin binding in its n‐region. We found that a signal peptide fragment of p‐gp160 was released into the cytosol and interacts with calmodulin. Our results suggest that signal peptide fragments of some cellular and viral proteins can interact with cytosolic target molecules. The functional consequences of such interactions remain to be established. However, our data suggest that signal sequences may be functionally more versatile than anticipated up to now. calmodulin (dpeaa)DE-He213 eukaryotic signal peptidase (dpeaa)DE-He213 HIV‐1 gp160 (dpeaa)DE-He213 prolactin secretion (dpeaa)DE-He213 signal sequence (dpeaa)DE-He213 Graf, Roland verfasserin aut Dobberstein, Bernhard verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 16(1997), 22 vom: 15. Nov., Seite 6636-6645 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:16 year:1997 number:22 day:15 month:11 pages:6636-6645 https://dx.doi.org/10.1093/emboj/16.22.6636 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER 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_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 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_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 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_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 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_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4318 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_4367 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 16 1997 22 15 11 6636-6645 |
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Enthalten in The EMBO Journal 16(1997), 22 vom: 15. Nov., Seite 6636-6645 volume:16 year:1997 number:22 day:15 month:11 pages:6636-6645 |
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Enthalten in The EMBO Journal 16(1997), 22 vom: 15. Nov., Seite 6636-6645 volume:16 year:1997 number:22 day:15 month:11 pages:6636-6645 |
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calmodulin eukaryotic signal peptidase HIV‐1 gp160 prolactin secretion signal sequence |
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Martoglio, Bruno @@aut@@ Graf, Roland @@aut@@ Dobberstein, Bernhard @@aut@@ |
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1997-11-15T00:00:00Z |
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| author |
Martoglio, Bruno |
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Martoglio, Bruno misc calmodulin misc eukaryotic signal peptidase misc HIV‐1 gp160 misc prolactin secretion misc signal sequence Signal peptide fragments of preprolactin and HIV‐1 p‐gp160 interact with calmodulin |
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Signal peptide fragments of preprolactin and HIV‐1 p‐gp160 interact with calmodulin calmodulin (dpeaa)DE-He213 eukaryotic signal peptidase (dpeaa)DE-He213 HIV‐1 gp160 (dpeaa)DE-He213 prolactin secretion (dpeaa)DE-He213 signal sequence (dpeaa)DE-He213 |
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misc calmodulin misc eukaryotic signal peptidase misc HIV‐1 gp160 misc prolactin secretion misc signal sequence |
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Signal peptide fragments of preprolactin and HIV‐1 p‐gp160 interact with calmodulin |
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Signal peptide fragments of preprolactin and HIV‐1 p‐gp160 interact with calmodulin |
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Martoglio, Bruno Graf, Roland Dobberstein, Bernhard |
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signal peptide fragments of preprolactin and hiv‐1 p‐gp160 interact with calmodulin |
| title_auth |
Signal peptide fragments of preprolactin and HIV‐1 p‐gp160 interact with calmodulin |
| abstract |
Abstract Secretory proteins and most membrane proteins are synthesized with a signal sequence that is usually cleaved from the nascent polypeptide during transport into the lumen of the endoplasmic reticulum. Using site‐specific photo‐crosslinking we have followed the fate of the signal sequence of preprolactin in a cell‐free system. This signal sequence has an unusually long hydrophilic n‐region containing several positively charged amino acid residues. We found that after cleavage by signal peptidase the signal sequence is in contact with lipids and subunits of the signal peptidase complex. The cleaved signal sequence is processed further and an N‐terminal fragment is released into the cytosol. This signal peptide fragment was found to interact efficiently with calmodulin. Similar to preprolactin, the signal sequence of the HIV‐1 envelope protein p‐gp160 has the characteristic feature for calmodulin binding in its n‐region. We found that a signal peptide fragment of p‐gp160 was released into the cytosol and interacts with calmodulin. Our results suggest that signal peptide fragments of some cellular and viral proteins can interact with cytosolic target molecules. The functional consequences of such interactions remain to be established. However, our data suggest that signal sequences may be functionally more versatile than anticipated up to now. © European Molecular Biology Organization 1997 |
| abstractGer |
Abstract Secretory proteins and most membrane proteins are synthesized with a signal sequence that is usually cleaved from the nascent polypeptide during transport into the lumen of the endoplasmic reticulum. Using site‐specific photo‐crosslinking we have followed the fate of the signal sequence of preprolactin in a cell‐free system. This signal sequence has an unusually long hydrophilic n‐region containing several positively charged amino acid residues. We found that after cleavage by signal peptidase the signal sequence is in contact with lipids and subunits of the signal peptidase complex. The cleaved signal sequence is processed further and an N‐terminal fragment is released into the cytosol. This signal peptide fragment was found to interact efficiently with calmodulin. Similar to preprolactin, the signal sequence of the HIV‐1 envelope protein p‐gp160 has the characteristic feature for calmodulin binding in its n‐region. We found that a signal peptide fragment of p‐gp160 was released into the cytosol and interacts with calmodulin. Our results suggest that signal peptide fragments of some cellular and viral proteins can interact with cytosolic target molecules. The functional consequences of such interactions remain to be established. However, our data suggest that signal sequences may be functionally more versatile than anticipated up to now. © European Molecular Biology Organization 1997 |
| abstract_unstemmed |
Abstract Secretory proteins and most membrane proteins are synthesized with a signal sequence that is usually cleaved from the nascent polypeptide during transport into the lumen of the endoplasmic reticulum. Using site‐specific photo‐crosslinking we have followed the fate of the signal sequence of preprolactin in a cell‐free system. This signal sequence has an unusually long hydrophilic n‐region containing several positively charged amino acid residues. We found that after cleavage by signal peptidase the signal sequence is in contact with lipids and subunits of the signal peptidase complex. The cleaved signal sequence is processed further and an N‐terminal fragment is released into the cytosol. This signal peptide fragment was found to interact efficiently with calmodulin. Similar to preprolactin, the signal sequence of the HIV‐1 envelope protein p‐gp160 has the characteristic feature for calmodulin binding in its n‐region. We found that a signal peptide fragment of p‐gp160 was released into the cytosol and interacts with calmodulin. Our results suggest that signal peptide fragments of some cellular and viral proteins can interact with cytosolic target molecules. The functional consequences of such interactions remain to be established. However, our data suggest that signal sequences may be functionally more versatile than anticipated up to now. © European Molecular Biology Organization 1997 |
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Signal peptide fragments of preprolactin and HIV‐1 p‐gp160 interact with calmodulin |
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https://dx.doi.org/10.1093/emboj/16.22.6636 |
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Graf, Roland Dobberstein, Bernhard |
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10.1093/emboj/16.22.6636 |
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| score |
7.4005814 |