Surface-exposed domains of TatB involved in the structural and functional assembly of the Tat translocase in Escherichia coli-Reference-Cited by-同舟云学术

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Surface-exposed domains of TatB involved in the structural and functional assembly of the Tat translocase in Escherichia coli

Published:2019-09 Issue:38 Volume:294 Page:13902-13914
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Fröbel Julia,Blümmel Anne-Sophie,Drepper Friedel,Warscheid Bettina,Müller Matthias

Funder

Deutsche Forschungsgemeinschaft (DFG)

Excellence Initiative of the German Federal and State Governments

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference59 articles.

1. The h-region of twin-arginine signal peptides supports productive binding of bacterial Tat precursor proteins to the TatBC receptor complex;Ulfig;J. Biol. Chem,2017

2. Signal peptide hydrophobicity modulates interaction with the twin-arginine translocase;Huang;MBio,2017

3. The early mature part of bacterial twin-arginine translocation (Tat) precursor proteins contributes to TatBC receptor binding;Ulfig;J. Biol. Chem,2018

4. Substrate-dependent assembly of the Tat translocase as observed in live Escherichia coli cells;Rose;PLoS One,2013

5. Live cell imaging shows reversible assembly of the TatA component of the twin-arginine protein transport system;Alcock;Proc. Natl. Acad. Sci. U.S.A,2013

Cited by 3 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. New insights into the Tat protein transport cycle from characterizing the assembled Tat translocon;Molecular Microbiology;2022-10-05

2. Oligomerization state of the functional bacterial twin-arginine translocation (Tat) receptor complex;Communications Biology;2022-09-19

3. Oligomerization state of the functional bacterial twin arginine translocation (Tat) receptor complex;2021-11-02

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