A crucial role of N-terminal domain of influenza A virus M1 protein in interaction with swine importin α1 protein
Abstract The matrix 1 (M1) protein is a multifunctional protein in the life cycle of influenza virus. It plays an important role in virus budding and intracellular trafficking of viral ribonucleoproteins (vRNPs). The M1 protein consists of three domains based on the structure: N-terminal domain, Mid...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Liu, Qinfang [verfasserIn] Bawa, Bhupinder [verfasserIn] Ma, Jingjiao [verfasserIn] Li, Feng [verfasserIn] Ma, Wenjun [verfasserIn] Richt, Jürgen A. [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2014 |
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| Schlagwörter: |
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| Übergeordnetes Werk: |
Enthalten in: Virus genes - Dordrecht [u.a.] : Springer Science + Business Media B.V, 1987, 49(2014), 1 vom: 18. Apr., Seite 157-162 |
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| Übergeordnetes Werk: |
volume:49 ; year:2014 ; number:1 ; day:18 ; month:04 ; pages:157-162 |
| Links: |
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| DOI / URN: |
10.1007/s11262-014-1068-6 |
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| Katalog-ID: |
SPR018770509 |
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| 100 | 1 | |a Liu, Qinfang |e verfasserin |4 aut | |
| 245 | 1 | 2 | |a A crucial role of N-terminal domain of influenza A virus M1 protein in interaction with swine importin α1 protein |
| 264 | 1 | |c 2014 | |
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| 520 | |a Abstract The matrix 1 (M1) protein is a multifunctional protein in the life cycle of influenza virus. It plays an important role in virus budding and intracellular trafficking of viral ribonucleoproteins (vRNPs). The M1 protein consists of three domains based on the structure: N-terminal domain, Middle domain, and C-terminal domain. However, the functions of different domains of the M1 protein remain largely unclear. In this study, using bimolecular fluorescence complementation assays (BIFC) we demonstrated that swine importin α1 interacts with the M1 protein and transports it to the nucleus. Interestingly, M1 with mutated nuclear localization signal (NLS; 101-RKLKR-105 to 101-AALAA-105) still interacts with swine importin α1 and is localized in the nucleus, suggesting that the NLS located at residues 101–105 is not the only NLS within M1 recombinant protein containing 1–160 residues of M1 with mutated nuclear localization signal is able to interact with swine importin α1, but M1/60-252 domains cannot bind importin α1. Further mapping showed that the deletion of residues 1–20 impaired the interaction between N terminus of M1 and importin α1. Collectively, our data suggested that the N-terminal domain of M1 protein is critical for binding swine importin α1 and for nuclear localization. | ||
| 650 | 4 | |a Influenza Virus |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Nuclear Localization Signal |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Nuclear Export Signal |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Middle Domain |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Nuclear Export Protein |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a Bawa, Bhupinder |e verfasserin |4 aut | |
| 700 | 1 | |a Ma, Jingjiao |e verfasserin |4 aut | |
| 700 | 1 | |a Li, Feng |e verfasserin |4 aut | |
| 700 | 1 | |a Ma, Wenjun |e verfasserin |4 aut | |
| 700 | 1 | |a Richt, Jürgen A. |e verfasserin |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t Virus genes |d Dordrecht [u.a.] : Springer Science + Business Media B.V, 1987 |g 49(2014), 1 vom: 18. Apr., Seite 157-162 |w (DE-627)320492052 |w (DE-600)2011138-1 |x 1572-994X |7 nnns |
| 773 | 1 | 8 | |g volume:49 |g year:2014 |g number:1 |g day:18 |g month:04 |g pages:157-162 |
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| 912 | |a GBV_ILN_2064 | ||
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10.1007/s11262-014-1068-6 doi (DE-627)SPR018770509 (SPR)s11262-014-1068-6-e DE-627 ger DE-627 rakwb eng 570 610 ASE 44.43 bkl Liu, Qinfang verfasserin aut A crucial role of N-terminal domain of influenza A virus M1 protein in interaction with swine importin α1 protein 2014 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract The matrix 1 (M1) protein is a multifunctional protein in the life cycle of influenza virus. It plays an important role in virus budding and intracellular trafficking of viral ribonucleoproteins (vRNPs). The M1 protein consists of three domains based on the structure: N-terminal domain, Middle domain, and C-terminal domain. However, the functions of different domains of the M1 protein remain largely unclear. In this study, using bimolecular fluorescence complementation assays (BIFC) we demonstrated that swine importin α1 interacts with the M1 protein and transports it to the nucleus. Interestingly, M1 with mutated nuclear localization signal (NLS; 101-RKLKR-105 to 101-AALAA-105) still interacts with swine importin α1 and is localized in the nucleus, suggesting that the NLS located at residues 101–105 is not the only NLS within M1 recombinant protein containing 1–160 residues of M1 with mutated nuclear localization signal is able to interact with swine importin α1, but M1/60-252 domains cannot bind importin α1. Further mapping showed that the deletion of residues 1–20 impaired the interaction between N terminus of M1 and importin α1. Collectively, our data suggested that the N-terminal domain of M1 protein is critical for binding swine importin α1 and for nuclear localization. Influenza Virus (dpeaa)DE-He213 Nuclear Localization Signal (dpeaa)DE-He213 Nuclear Export Signal (dpeaa)DE-He213 Middle Domain (dpeaa)DE-He213 Nuclear Export Protein (dpeaa)DE-He213 Bawa, Bhupinder verfasserin aut Ma, Jingjiao verfasserin aut Li, Feng verfasserin aut Ma, Wenjun verfasserin aut Richt, Jürgen A. verfasserin aut Enthalten in Virus genes Dordrecht [u.a.] : Springer Science + Business Media B.V, 1987 49(2014), 1 vom: 18. Apr., Seite 157-162 (DE-627)320492052 (DE-600)2011138-1 1572-994X nnns volume:49 year:2014 number:1 day:18 month:04 pages:157-162 https://dx.doi.org/10.1007/s11262-014-1068-6 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_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_252 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 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_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_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 44.43 ASE AR 49 2014 1 18 04 157-162 |
| spelling |
10.1007/s11262-014-1068-6 doi (DE-627)SPR018770509 (SPR)s11262-014-1068-6-e DE-627 ger DE-627 rakwb eng 570 610 ASE 44.43 bkl Liu, Qinfang verfasserin aut A crucial role of N-terminal domain of influenza A virus M1 protein in interaction with swine importin α1 protein 2014 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract The matrix 1 (M1) protein is a multifunctional protein in the life cycle of influenza virus. It plays an important role in virus budding and intracellular trafficking of viral ribonucleoproteins (vRNPs). The M1 protein consists of three domains based on the structure: N-terminal domain, Middle domain, and C-terminal domain. However, the functions of different domains of the M1 protein remain largely unclear. In this study, using bimolecular fluorescence complementation assays (BIFC) we demonstrated that swine importin α1 interacts with the M1 protein and transports it to the nucleus. Interestingly, M1 with mutated nuclear localization signal (NLS; 101-RKLKR-105 to 101-AALAA-105) still interacts with swine importin α1 and is localized in the nucleus, suggesting that the NLS located at residues 101–105 is not the only NLS within M1 recombinant protein containing 1–160 residues of M1 with mutated nuclear localization signal is able to interact with swine importin α1, but M1/60-252 domains cannot bind importin α1. Further mapping showed that the deletion of residues 1–20 impaired the interaction between N terminus of M1 and importin α1. Collectively, our data suggested that the N-terminal domain of M1 protein is critical for binding swine importin α1 and for nuclear localization. Influenza Virus (dpeaa)DE-He213 Nuclear Localization Signal (dpeaa)DE-He213 Nuclear Export Signal (dpeaa)DE-He213 Middle Domain (dpeaa)DE-He213 Nuclear Export Protein (dpeaa)DE-He213 Bawa, Bhupinder verfasserin aut Ma, Jingjiao verfasserin aut Li, Feng verfasserin aut Ma, Wenjun verfasserin aut Richt, Jürgen A. verfasserin aut Enthalten in Virus genes Dordrecht [u.a.] : Springer Science + Business Media B.V, 1987 49(2014), 1 vom: 18. Apr., Seite 157-162 (DE-627)320492052 (DE-600)2011138-1 1572-994X nnns volume:49 year:2014 number:1 day:18 month:04 pages:157-162 https://dx.doi.org/10.1007/s11262-014-1068-6 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_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_252 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 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_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_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 44.43 ASE AR 49 2014 1 18 04 157-162 |
| allfields_unstemmed |
10.1007/s11262-014-1068-6 doi (DE-627)SPR018770509 (SPR)s11262-014-1068-6-e DE-627 ger DE-627 rakwb eng 570 610 ASE 44.43 bkl Liu, Qinfang verfasserin aut A crucial role of N-terminal domain of influenza A virus M1 protein in interaction with swine importin α1 protein 2014 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract The matrix 1 (M1) protein is a multifunctional protein in the life cycle of influenza virus. It plays an important role in virus budding and intracellular trafficking of viral ribonucleoproteins (vRNPs). The M1 protein consists of three domains based on the structure: N-terminal domain, Middle domain, and C-terminal domain. However, the functions of different domains of the M1 protein remain largely unclear. In this study, using bimolecular fluorescence complementation assays (BIFC) we demonstrated that swine importin α1 interacts with the M1 protein and transports it to the nucleus. Interestingly, M1 with mutated nuclear localization signal (NLS; 101-RKLKR-105 to 101-AALAA-105) still interacts with swine importin α1 and is localized in the nucleus, suggesting that the NLS located at residues 101–105 is not the only NLS within M1 recombinant protein containing 1–160 residues of M1 with mutated nuclear localization signal is able to interact with swine importin α1, but M1/60-252 domains cannot bind importin α1. Further mapping showed that the deletion of residues 1–20 impaired the interaction between N terminus of M1 and importin α1. Collectively, our data suggested that the N-terminal domain of M1 protein is critical for binding swine importin α1 and for nuclear localization. Influenza Virus (dpeaa)DE-He213 Nuclear Localization Signal (dpeaa)DE-He213 Nuclear Export Signal (dpeaa)DE-He213 Middle Domain (dpeaa)DE-He213 Nuclear Export Protein (dpeaa)DE-He213 Bawa, Bhupinder verfasserin aut Ma, Jingjiao verfasserin aut Li, Feng verfasserin aut Ma, Wenjun verfasserin aut Richt, Jürgen A. verfasserin aut Enthalten in Virus genes Dordrecht [u.a.] : Springer Science + Business Media B.V, 1987 49(2014), 1 vom: 18. Apr., Seite 157-162 (DE-627)320492052 (DE-600)2011138-1 1572-994X nnns volume:49 year:2014 number:1 day:18 month:04 pages:157-162 https://dx.doi.org/10.1007/s11262-014-1068-6 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_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_252 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 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_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_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 44.43 ASE AR 49 2014 1 18 04 157-162 |
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10.1007/s11262-014-1068-6 doi (DE-627)SPR018770509 (SPR)s11262-014-1068-6-e DE-627 ger DE-627 rakwb eng 570 610 ASE 44.43 bkl Liu, Qinfang verfasserin aut A crucial role of N-terminal domain of influenza A virus M1 protein in interaction with swine importin α1 protein 2014 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract The matrix 1 (M1) protein is a multifunctional protein in the life cycle of influenza virus. It plays an important role in virus budding and intracellular trafficking of viral ribonucleoproteins (vRNPs). The M1 protein consists of three domains based on the structure: N-terminal domain, Middle domain, and C-terminal domain. However, the functions of different domains of the M1 protein remain largely unclear. In this study, using bimolecular fluorescence complementation assays (BIFC) we demonstrated that swine importin α1 interacts with the M1 protein and transports it to the nucleus. Interestingly, M1 with mutated nuclear localization signal (NLS; 101-RKLKR-105 to 101-AALAA-105) still interacts with swine importin α1 and is localized in the nucleus, suggesting that the NLS located at residues 101–105 is not the only NLS within M1 recombinant protein containing 1–160 residues of M1 with mutated nuclear localization signal is able to interact with swine importin α1, but M1/60-252 domains cannot bind importin α1. Further mapping showed that the deletion of residues 1–20 impaired the interaction between N terminus of M1 and importin α1. Collectively, our data suggested that the N-terminal domain of M1 protein is critical for binding swine importin α1 and for nuclear localization. Influenza Virus (dpeaa)DE-He213 Nuclear Localization Signal (dpeaa)DE-He213 Nuclear Export Signal (dpeaa)DE-He213 Middle Domain (dpeaa)DE-He213 Nuclear Export Protein (dpeaa)DE-He213 Bawa, Bhupinder verfasserin aut Ma, Jingjiao verfasserin aut Li, Feng verfasserin aut Ma, Wenjun verfasserin aut Richt, Jürgen A. verfasserin aut Enthalten in Virus genes Dordrecht [u.a.] : Springer Science + Business Media B.V, 1987 49(2014), 1 vom: 18. Apr., Seite 157-162 (DE-627)320492052 (DE-600)2011138-1 1572-994X nnns volume:49 year:2014 number:1 day:18 month:04 pages:157-162 https://dx.doi.org/10.1007/s11262-014-1068-6 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_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_252 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 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_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_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 44.43 ASE AR 49 2014 1 18 04 157-162 |
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10.1007/s11262-014-1068-6 doi (DE-627)SPR018770509 (SPR)s11262-014-1068-6-e DE-627 ger DE-627 rakwb eng 570 610 ASE 44.43 bkl Liu, Qinfang verfasserin aut A crucial role of N-terminal domain of influenza A virus M1 protein in interaction with swine importin α1 protein 2014 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract The matrix 1 (M1) protein is a multifunctional protein in the life cycle of influenza virus. It plays an important role in virus budding and intracellular trafficking of viral ribonucleoproteins (vRNPs). The M1 protein consists of three domains based on the structure: N-terminal domain, Middle domain, and C-terminal domain. However, the functions of different domains of the M1 protein remain largely unclear. In this study, using bimolecular fluorescence complementation assays (BIFC) we demonstrated that swine importin α1 interacts with the M1 protein and transports it to the nucleus. Interestingly, M1 with mutated nuclear localization signal (NLS; 101-RKLKR-105 to 101-AALAA-105) still interacts with swine importin α1 and is localized in the nucleus, suggesting that the NLS located at residues 101–105 is not the only NLS within M1 recombinant protein containing 1–160 residues of M1 with mutated nuclear localization signal is able to interact with swine importin α1, but M1/60-252 domains cannot bind importin α1. Further mapping showed that the deletion of residues 1–20 impaired the interaction between N terminus of M1 and importin α1. Collectively, our data suggested that the N-terminal domain of M1 protein is critical for binding swine importin α1 and for nuclear localization. Influenza Virus (dpeaa)DE-He213 Nuclear Localization Signal (dpeaa)DE-He213 Nuclear Export Signal (dpeaa)DE-He213 Middle Domain (dpeaa)DE-He213 Nuclear Export Protein (dpeaa)DE-He213 Bawa, Bhupinder verfasserin aut Ma, Jingjiao verfasserin aut Li, Feng verfasserin aut Ma, Wenjun verfasserin aut Richt, Jürgen A. verfasserin aut Enthalten in Virus genes Dordrecht [u.a.] : Springer Science + Business Media B.V, 1987 49(2014), 1 vom: 18. Apr., Seite 157-162 (DE-627)320492052 (DE-600)2011138-1 1572-994X nnns volume:49 year:2014 number:1 day:18 month:04 pages:157-162 https://dx.doi.org/10.1007/s11262-014-1068-6 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_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_252 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 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_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_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 44.43 ASE AR 49 2014 1 18 04 157-162 |
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English |
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Enthalten in Virus genes 49(2014), 1 vom: 18. Apr., Seite 157-162 volume:49 year:2014 number:1 day:18 month:04 pages:157-162 |
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Enthalten in Virus genes 49(2014), 1 vom: 18. Apr., Seite 157-162 volume:49 year:2014 number:1 day:18 month:04 pages:157-162 |
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findex.gbv.de |
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Influenza Virus Nuclear Localization Signal Nuclear Export Signal Middle Domain Nuclear Export Protein |
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Virus genes |
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Liu, Qinfang @@aut@@ Bawa, Bhupinder @@aut@@ Ma, Jingjiao @@aut@@ Li, Feng @@aut@@ Ma, Wenjun @@aut@@ Richt, Jürgen A. @@aut@@ |
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2014-04-18T00:00:00Z |
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It plays an important role in virus budding and intracellular trafficking of viral ribonucleoproteins (vRNPs). The M1 protein consists of three domains based on the structure: N-terminal domain, Middle domain, and C-terminal domain. However, the functions of different domains of the M1 protein remain largely unclear. In this study, using bimolecular fluorescence complementation assays (BIFC) we demonstrated that swine importin α1 interacts with the M1 protein and transports it to the nucleus. Interestingly, M1 with mutated nuclear localization signal (NLS; 101-RKLKR-105 to 101-AALAA-105) still interacts with swine importin α1 and is localized in the nucleus, suggesting that the NLS located at residues 101–105 is not the only NLS within M1 recombinant protein containing 1–160 residues of M1 with mutated nuclear localization signal is able to interact with swine importin α1, but M1/60-252 domains cannot bind importin α1. Further mapping showed that the deletion of residues 1–20 impaired the interaction between N terminus of M1 and importin α1. Collectively, our data suggested that the N-terminal domain of M1 protein is critical for binding swine importin α1 and for nuclear localization.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Influenza Virus</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Nuclear Localization Signal</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Nuclear Export Signal</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Middle Domain</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Nuclear Export Protein</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Bawa, Bhupinder</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Ma, Jingjiao</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Li, Feng</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Ma, Wenjun</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Richt, Jürgen A.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">Virus genes</subfield><subfield code="d">Dordrecht [u.a.] : Springer Science + Business Media B.V, 1987</subfield><subfield code="g">49(2014), 1 vom: 18. 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|
| author |
Liu, Qinfang |
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Liu, Qinfang ddc 570 bkl 44.43 misc Influenza Virus misc Nuclear Localization Signal misc Nuclear Export Signal misc Middle Domain misc Nuclear Export Protein A crucial role of N-terminal domain of influenza A virus M1 protein in interaction with swine importin α1 protein |
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570 610 ASE 44.43 bkl A crucial role of N-terminal domain of influenza A virus M1 protein in interaction with swine importin α1 protein Influenza Virus (dpeaa)DE-He213 Nuclear Localization Signal (dpeaa)DE-He213 Nuclear Export Signal (dpeaa)DE-He213 Middle Domain (dpeaa)DE-He213 Nuclear Export Protein (dpeaa)DE-He213 |
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ddc 570 bkl 44.43 misc Influenza Virus misc Nuclear Localization Signal misc Nuclear Export Signal misc Middle Domain misc Nuclear Export Protein |
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ddc 570 bkl 44.43 misc Influenza Virus misc Nuclear Localization Signal misc Nuclear Export Signal misc Middle Domain misc Nuclear Export Protein |
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ddc 570 bkl 44.43 misc Influenza Virus misc Nuclear Localization Signal misc Nuclear Export Signal misc Middle Domain misc Nuclear Export Protein |
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A crucial role of N-terminal domain of influenza A virus M1 protein in interaction with swine importin α1 protein |
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A crucial role of N-terminal domain of influenza A virus M1 protein in interaction with swine importin α1 protein |
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Liu, Qinfang |
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Liu, Qinfang Bawa, Bhupinder Ma, Jingjiao Li, Feng Ma, Wenjun Richt, Jürgen A. |
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crucial role of n-terminal domain of influenza a virus m1 protein in interaction with swine importin α1 protein |
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A crucial role of N-terminal domain of influenza A virus M1 protein in interaction with swine importin α1 protein |
| abstract |
Abstract The matrix 1 (M1) protein is a multifunctional protein in the life cycle of influenza virus. It plays an important role in virus budding and intracellular trafficking of viral ribonucleoproteins (vRNPs). The M1 protein consists of three domains based on the structure: N-terminal domain, Middle domain, and C-terminal domain. However, the functions of different domains of the M1 protein remain largely unclear. In this study, using bimolecular fluorescence complementation assays (BIFC) we demonstrated that swine importin α1 interacts with the M1 protein and transports it to the nucleus. Interestingly, M1 with mutated nuclear localization signal (NLS; 101-RKLKR-105 to 101-AALAA-105) still interacts with swine importin α1 and is localized in the nucleus, suggesting that the NLS located at residues 101–105 is not the only NLS within M1 recombinant protein containing 1–160 residues of M1 with mutated nuclear localization signal is able to interact with swine importin α1, but M1/60-252 domains cannot bind importin α1. Further mapping showed that the deletion of residues 1–20 impaired the interaction between N terminus of M1 and importin α1. Collectively, our data suggested that the N-terminal domain of M1 protein is critical for binding swine importin α1 and for nuclear localization. |
| abstractGer |
Abstract The matrix 1 (M1) protein is a multifunctional protein in the life cycle of influenza virus. It plays an important role in virus budding and intracellular trafficking of viral ribonucleoproteins (vRNPs). The M1 protein consists of three domains based on the structure: N-terminal domain, Middle domain, and C-terminal domain. However, the functions of different domains of the M1 protein remain largely unclear. In this study, using bimolecular fluorescence complementation assays (BIFC) we demonstrated that swine importin α1 interacts with the M1 protein and transports it to the nucleus. Interestingly, M1 with mutated nuclear localization signal (NLS; 101-RKLKR-105 to 101-AALAA-105) still interacts with swine importin α1 and is localized in the nucleus, suggesting that the NLS located at residues 101–105 is not the only NLS within M1 recombinant protein containing 1–160 residues of M1 with mutated nuclear localization signal is able to interact with swine importin α1, but M1/60-252 domains cannot bind importin α1. Further mapping showed that the deletion of residues 1–20 impaired the interaction between N terminus of M1 and importin α1. Collectively, our data suggested that the N-terminal domain of M1 protein is critical for binding swine importin α1 and for nuclear localization. |
| abstract_unstemmed |
Abstract The matrix 1 (M1) protein is a multifunctional protein in the life cycle of influenza virus. It plays an important role in virus budding and intracellular trafficking of viral ribonucleoproteins (vRNPs). The M1 protein consists of three domains based on the structure: N-terminal domain, Middle domain, and C-terminal domain. However, the functions of different domains of the M1 protein remain largely unclear. In this study, using bimolecular fluorescence complementation assays (BIFC) we demonstrated that swine importin α1 interacts with the M1 protein and transports it to the nucleus. Interestingly, M1 with mutated nuclear localization signal (NLS; 101-RKLKR-105 to 101-AALAA-105) still interacts with swine importin α1 and is localized in the nucleus, suggesting that the NLS located at residues 101–105 is not the only NLS within M1 recombinant protein containing 1–160 residues of M1 with mutated nuclear localization signal is able to interact with swine importin α1, but M1/60-252 domains cannot bind importin α1. Further mapping showed that the deletion of residues 1–20 impaired the interaction between N terminus of M1 and importin α1. Collectively, our data suggested that the N-terminal domain of M1 protein is critical for binding swine importin α1 and for nuclear localization. |
| collection_details |
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| container_issue |
1 |
| title_short |
A crucial role of N-terminal domain of influenza A virus M1 protein in interaction with swine importin α1 protein |
| url |
https://dx.doi.org/10.1007/s11262-014-1068-6 |
| remote_bool |
true |
| author2 |
Bawa, Bhupinder Ma, Jingjiao Li, Feng Ma, Wenjun Richt, Jürgen A. |
| author2Str |
Bawa, Bhupinder Ma, Jingjiao Li, Feng Ma, Wenjun Richt, Jürgen A. |
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| doi_str |
10.1007/s11262-014-1068-6 |
| up_date |
2024-07-03T22:06:11.187Z |
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| score |
7.399766 |