Category:Complex:TatABCE protein export complex: Difference between revisions

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==About==
'''Description''' (originally from EcoCyc<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>) TatABCE protein export complex
 
'''Comments''' (originally from EcoCyc<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>) The twin-arginine translocation (Tat) system works in parallel with the <I>E. coli</I> Sec translocation system to
transport folded proteins across the cytoplasmic membrane <ref name='PMID:9546395'/><ref name='PMID:11004447'/><ref name='PMID:9649434'/><ref name='PMID:11099493'/><ref name='PMID:9660752'/><ref name='PMID:11591389'/><ref name='PMID:9649434'/><ref name='PMID:11922668'/><ref name='PMID:9660752'/><ref name='PMID:10747959'/><ref name='PMID:1648086'/><ref name='PMID:15225613'/><ref name='PMID:16092529'/>
 
 
==References==
<references/>

Revision as of 12:26, 20 July 2007

About

Description (originally from EcoCyc[1][2]) TatABCE protein export complex

Comments (originally from EcoCyc[1][2]) The twin-arginine translocation (Tat) system works in parallel with the E. coli Sec translocation system to transport folded proteins across the cytoplasmic membrane [3][4][5][6][7][8][5][9][7][10][11][12][13]


References

  1. ↑ 1.0 1.1 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  2. ↑ 2.0 2.1 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. ↑ Weiner, JH et al. (1998) A novel and ubiquitous system for membrane targeting and secretion of cofactor-containing proteins. Cell 93 93-101 PubMed
  4. ↑ Berks, BC et al. (2000) A novel protein transport system involved in the biogenesis of bacterial electron transfer chains. Biochim Biophys Acta 1459 325-30 PubMed
  5. ↑ 5.0 5.1 Sargent, F et al. (1998) Overlapping functions of components of a bacterial Sec-independent protein export pathway. EMBO J. 17 3640-50 PubMed
  6. ↑ Santini, CL et al. (2001) Translocation of jellyfish green fluorescent protein via the Tat system of Escherichia coli and change of its periplasmic localization in response to osmotic up-shock. J Biol Chem 276 8159-64 PubMed
  7. ↑ 7.0 7.1 Bogsch, EG et al. (1998) An essential component of a novel bacterial protein export system with homologues in plastids and mitochondria. J. Biol. Chem. 273 18003-6 PubMed
  8. ↑ De Leeuw, E et al. (2001) Membrane interactions and self-association of the TatA and TatB components of the twin-arginine translocation pathway. FEBS Lett 506 143-8 PubMed
  9. ↑ Ize, B et al. (2002) In vivo dissection of the Tat translocation pathway in Escherichia coli. J Mol Biol 317 327-35 PubMed
  10. ↑ Wexler, M et al. (2000) TatD is a cytoplasmic protein with DNase activity. No requirement for TatD family proteins in sec-independent protein export. J. Biol. Chem. 275 16717-22 PubMed
  11. ↑ Mould, RM & Robinson, C (1991) A proton gradient is required for the transport of two lumenal oxygen-evolving proteins across the thylakoid membrane. J Biol Chem 266 12189-93 PubMed
  12. ↑ Berthelmann, F & Brüser, T (2004) Localization of the Tat translocon components in Escherichia coli. FEBS Lett 569 82-8 PubMed
  13. ↑ Müller, M & Klösgen, RB (2005) The Tat pathway in bacteria and chloroplasts (review). Mol Membr Biol 22 113-21 PubMed

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