Literature DB >> 16092529

The Tat pathway in bacteria and chloroplasts (review).

Matthias Müller1, Ralf Bernd Klösgen.   

Abstract

Both in prokaryotic organisms and in chloroplasts, a specialized protein transport pathway exists which is capable of translocating proteins in a fully folded conformation. Transport is mediated in both instances by signal peptides harbouring a twin-arginine consensus motif (twin-arginine translocation (Tat) pathway). The Tat translocase comprises the three functionally different membrane proteins TatA, TatB, and TatC. While TatB and TatC are involved in the specific recognition of the substrate, TatA might be the major pore-forming component. Current evidence suggests that a functional Tat translocase is assembled from separate TatBC and TatA assemblies only on demand, i.e., in the presence of transport substrate and a transmembrane H+-motive force.

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Year:  2005        PMID: 16092529     DOI: 10.1080/09687860500041809

Source DB:  PubMed          Journal:  Mol Membr Biol        ISSN: 0968-7688            Impact factor:   2.857


  26 in total

1.  Multiple precursor proteins bind individual Tat receptor complexes and are collectively transported.

Authors:  Xianyue Ma; Kenneth Cline
Journal:  EMBO J       Date:  2010-03-25       Impact factor: 11.598

Review 2.  Protein secretion and membrane insertion systems in gram-negative bacteria.

Authors:  Milton H Saier
Journal:  J Membr Biol       Date:  2007-06-02       Impact factor: 1.843

3.  Genome of the opportunistic pathogen Streptococcus sanguinis.

Authors:  Ping Xu; Joao M Alves; Todd Kitten; Arunsri Brown; Zhenming Chen; Luiz S Ozaki; Patricio Manque; Xiuchun Ge; Myrna G Serrano; Daniela Puiu; Stephanie Hendricks; Yingping Wang; Michael D Chaplin; Doruk Akan; Sehmi Paik; Darrell L Peterson; Francis L Macrina; Gregory A Buck
Journal:  J Bacteriol       Date:  2007-02-02       Impact factor: 3.490

4.  Structure of the twin-arginine signal-binding protein DmsD from Escherichia coli.

Authors:  Suresh Kumar Ramasamy; William M Clemons
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2009-07-21

5.  A stromal pool of TatA promotes Tat-dependent protein transport across the thylakoid membrane.

Authors:  Stefan Frielingsdorf; Mario Jakob; Ralf Bernd Klösgen
Journal:  J Biol Chem       Date:  2008-10-07       Impact factor: 5.157

6.  Direct interaction between a precursor mature domain and transport component Tha4 during twin arginine transport of chloroplasts.

Authors:  Debjani Pal; Kristen Fite; Carole Dabney-Smith
Journal:  Plant Physiol       Date:  2012-12-03       Impact factor: 8.340

7.  Twin-arginine translocase mutations that suppress folding quality control and permit export of misfolded substrate proteins.

Authors:  Mark A Rocco; Dujduan Waraho-Zhmayev; Matthew P DeLisa
Journal:  Proc Natl Acad Sci U S A       Date:  2012-07-30       Impact factor: 11.205

8.  Functional analysis of the twin-arginine translocation pathway in Corynebacterium glutamicum ATCC 13869.

Authors:  Yoshimi Kikuchi; Masayo Date; Hiroshi Itaya; Kazuhiko Matsui; Long-Fei Wu
Journal:  Appl Environ Microbiol       Date:  2006-09-22       Impact factor: 4.792

9.  TatABC overexpression improves Corynebacterium glutamicum Tat-dependent protein secretion.

Authors:  Yoshimi Kikuchi; Hiroshi Itaya; Masayo Date; Kazuhiko Matsui; Long-Fei Wu
Journal:  Appl Environ Microbiol       Date:  2008-12-12       Impact factor: 4.792

10.  XA27 depends on an amino-terminal signal-anchor-like sequence to localize to the apoplast for resistance to Xanthomonas oryzae pv oryzae.

Authors:  Lifang Wu; Mei Ling Goh; Chellamma Sreekala; Zhongchao Yin
Journal:  Plant Physiol       Date:  2008-09-10       Impact factor: 8.340

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