The Tat protein export pathway
The Tat (twin-arginine translocation) system is a bacterial protein export pathway with the remarkable ability to transport folded proteins across the cytoplasmic membrane. Preproteins are directed to the Tat pathway by signal peptides that bear a characteristic sequence motif, which includes consec...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Berks, Ben C. [verfasserIn] Sargent, Frank [verfasserIn] Palmer, Tracy [verfasserIn] |
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| Format: |
E-Artikel |
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| Erschienen: |
Oxford BSL: Blackwell Science Ltd ; 2000 |
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| Umfang: |
Online-Ressource |
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| Reproduktion: |
2002 ; Blackwell Publishing Journal Backfiles 1879-2005 |
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| Übergeordnetes Werk: |
In: Molecular microbiology - Oxford [u.a.] : Wiley-Blackwell, 1987, 35(2000), 2, Seite 0 |
| Übergeordnetes Werk: |
volume:35 ; year:2000 ; number:2 ; pages:0 |
| Links: |
|---|
| DOI / URN: |
10.1046/j.1365-2958.2000.01719.x |
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NLEJ243569874 |
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| 520 | |a The Tat (twin-arginine translocation) system is a bacterial protein export pathway with the remarkable ability to transport folded proteins across the cytoplasmic membrane. Preproteins are directed to the Tat pathway by signal peptides that bear a characteristic sequence motif, which includes consecutive arginine residues. Here, we review recent progress on the characterization of the Tat system and critically discuss the structure and operation of this major new bacterial protein export pathway. | ||
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10.1046/j.1365-2958.2000.01719.x doi (DE-627)NLEJ243569874 DE-627 ger DE-627 rakwb Berks, Ben C. verfasserin aut The Tat protein export pathway Oxford BSL Blackwell Science Ltd 2000 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The Tat (twin-arginine translocation) system is a bacterial protein export pathway with the remarkable ability to transport folded proteins across the cytoplasmic membrane. Preproteins are directed to the Tat pathway by signal peptides that bear a characteristic sequence motif, which includes consecutive arginine residues. Here, we review recent progress on the characterization of the Tat system and critically discuss the structure and operation of this major new bacterial protein export pathway. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| Sargent, Frank verfasserin aut Palmer, Tracy verfasserin aut In Molecular microbiology Oxford [u.a.] : Wiley-Blackwell, 1987 35(2000), 2, Seite 0 Online-Ressource (DE-627)NLEJ243926537 (DE-600)1501537-3 1365-2958 nnns volume:35 year:2000 number:2 pages:0 http://dx.doi.org/10.1046/j.1365-2958.2000.01719.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 35 2000 2 0 |
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10.1046/j.1365-2958.2000.01719.x doi (DE-627)NLEJ243569874 DE-627 ger DE-627 rakwb Berks, Ben C. verfasserin aut The Tat protein export pathway Oxford BSL Blackwell Science Ltd 2000 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The Tat (twin-arginine translocation) system is a bacterial protein export pathway with the remarkable ability to transport folded proteins across the cytoplasmic membrane. Preproteins are directed to the Tat pathway by signal peptides that bear a characteristic sequence motif, which includes consecutive arginine residues. Here, we review recent progress on the characterization of the Tat system and critically discuss the structure and operation of this major new bacterial protein export pathway. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| Sargent, Frank verfasserin aut Palmer, Tracy verfasserin aut In Molecular microbiology Oxford [u.a.] : Wiley-Blackwell, 1987 35(2000), 2, Seite 0 Online-Ressource (DE-627)NLEJ243926537 (DE-600)1501537-3 1365-2958 nnns volume:35 year:2000 number:2 pages:0 http://dx.doi.org/10.1046/j.1365-2958.2000.01719.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 35 2000 2 0 |
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10.1046/j.1365-2958.2000.01719.x doi (DE-627)NLEJ243569874 DE-627 ger DE-627 rakwb Berks, Ben C. verfasserin aut The Tat protein export pathway Oxford BSL Blackwell Science Ltd 2000 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The Tat (twin-arginine translocation) system is a bacterial protein export pathway with the remarkable ability to transport folded proteins across the cytoplasmic membrane. Preproteins are directed to the Tat pathway by signal peptides that bear a characteristic sequence motif, which includes consecutive arginine residues. Here, we review recent progress on the characterization of the Tat system and critically discuss the structure and operation of this major new bacterial protein export pathway. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| Sargent, Frank verfasserin aut Palmer, Tracy verfasserin aut In Molecular microbiology Oxford [u.a.] : Wiley-Blackwell, 1987 35(2000), 2, Seite 0 Online-Ressource (DE-627)NLEJ243926537 (DE-600)1501537-3 1365-2958 nnns volume:35 year:2000 number:2 pages:0 http://dx.doi.org/10.1046/j.1365-2958.2000.01719.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 35 2000 2 0 |
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10.1046/j.1365-2958.2000.01719.x doi (DE-627)NLEJ243569874 DE-627 ger DE-627 rakwb Berks, Ben C. verfasserin aut The Tat protein export pathway Oxford BSL Blackwell Science Ltd 2000 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The Tat (twin-arginine translocation) system is a bacterial protein export pathway with the remarkable ability to transport folded proteins across the cytoplasmic membrane. Preproteins are directed to the Tat pathway by signal peptides that bear a characteristic sequence motif, which includes consecutive arginine residues. Here, we review recent progress on the characterization of the Tat system and critically discuss the structure and operation of this major new bacterial protein export pathway. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| Sargent, Frank verfasserin aut Palmer, Tracy verfasserin aut In Molecular microbiology Oxford [u.a.] : Wiley-Blackwell, 1987 35(2000), 2, Seite 0 Online-Ressource (DE-627)NLEJ243926537 (DE-600)1501537-3 1365-2958 nnns volume:35 year:2000 number:2 pages:0 http://dx.doi.org/10.1046/j.1365-2958.2000.01719.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 35 2000 2 0 |
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10.1046/j.1365-2958.2000.01719.x doi (DE-627)NLEJ243569874 DE-627 ger DE-627 rakwb Berks, Ben C. verfasserin aut The Tat protein export pathway Oxford BSL Blackwell Science Ltd 2000 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The Tat (twin-arginine translocation) system is a bacterial protein export pathway with the remarkable ability to transport folded proteins across the cytoplasmic membrane. Preproteins are directed to the Tat pathway by signal peptides that bear a characteristic sequence motif, which includes consecutive arginine residues. Here, we review recent progress on the characterization of the Tat system and critically discuss the structure and operation of this major new bacterial protein export pathway. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| Sargent, Frank verfasserin aut Palmer, Tracy verfasserin aut In Molecular microbiology Oxford [u.a.] : Wiley-Blackwell, 1987 35(2000), 2, Seite 0 Online-Ressource (DE-627)NLEJ243926537 (DE-600)1501537-3 1365-2958 nnns volume:35 year:2000 number:2 pages:0 http://dx.doi.org/10.1046/j.1365-2958.2000.01719.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 35 2000 2 0 |
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The Tat (twin-arginine translocation) system is a bacterial protein export pathway with the remarkable ability to transport folded proteins across the cytoplasmic membrane. Preproteins are directed to the Tat pathway by signal peptides that bear a characteristic sequence motif, which includes consecutive arginine residues. Here, we review recent progress on the characterization of the Tat system and critically discuss the structure and operation of this major new bacterial protein export pathway. |
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The Tat (twin-arginine translocation) system is a bacterial protein export pathway with the remarkable ability to transport folded proteins across the cytoplasmic membrane. Preproteins are directed to the Tat pathway by signal peptides that bear a characteristic sequence motif, which includes consecutive arginine residues. Here, we review recent progress on the characterization of the Tat system and critically discuss the structure and operation of this major new bacterial protein export pathway. |
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The Tat (twin-arginine translocation) system is a bacterial protein export pathway with the remarkable ability to transport folded proteins across the cytoplasmic membrane. Preproteins are directed to the Tat pathway by signal peptides that bear a characteristic sequence motif, which includes consecutive arginine residues. Here, we review recent progress on the characterization of the Tat system and critically discuss the structure and operation of this major new bacterial protein export pathway. |
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