Structural plasticity of the Salmonella FliS flagellar export chaperone-Reference-Cited by-同舟云学术

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Structural plasticity of the Salmonella FliS flagellar export chaperone

Published:2016-03-31 Issue:8 Volume:590 Page:1103-1113
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:FEBS Lett

Author:

Sajó Ráchel¹,Tőke Orsolya²,Hajdú István¹,Jankovics Hajnalka³,Micsonai András⁴,Dobó József¹,Kardos József⁴,Vonderviszt Ferenc³⁵

Affiliation:

1. Institute of Enzymology; Research Centre for Natural Sciences; Hungarian Academy of Sciences; Budapest Hungary

2. Institute of Organic Chemistry; Research Centre for Natural Sciences; Hungarian Academy of Sciences; Budapest Hungary

3. Bio-Nanosystems Laboratory; Research Institute for Chemical and Process Engineering; University of Pannonia; Veszprém Hungary

4. MTA-ELTE NAP B Neuroimmunology Research Group; Department of Biochemistry; Institute of Biology; Eötvös Loránd University; Budapest Hungary

5. Institute of Technical Physics and Materials Science; Centre for Energy Research; Hungarian Academy of Sciences; Budapest Hungary

Funder

Japan Science and Technology Corporation

Országos Tudományos Kutatási Alapprogramok

SOLEIL

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/1873-3468.12149/fullpdf

Reference46 articles.

1. Protein export through the bacterial type III export pathway;Minamino;Biochim Biophys Acta,2014

2. Flagellin polymerisation control by a cytosolic export chaperone;Auvray;J Mol Biol,2001

3. Substrate-specific binding of hook-associated proteins by FlgN and FliT, putative chaperones for flagellum assembly;Fraser;Mol Microbiol,1999

4. From flagellum assembly to virulence: the extended family of type III export chaperones;Bennett;Trends Microbiol,2000

5. Docking of cytosolic chaperone-substrate complexes at the membrane ATPase during flagellar type III protein export;Thomas;Proc Natl Acad Sci USA,2004

Cited by 5 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. The protein-binding N-terminal domain of human translation elongation factor 1Bβ possesses a dynamic α-helical structural organization;International Journal of Biological Macromolecules;2019-04

2. BeStSel: a web server for accurate protein secondary structure prediction and fold recognition from the circular dichroism spectra;Nucleic Acids Research;2018-06-11

3. Proline hydroxylation at different sites in hypoxia-inducible factor 1α modulates its interactions with the von Hippel–Lindau tumor suppressor protein;Physical Chemistry Chemical Physics;2018

4. Structural stability of flagellin subunit affects the rate of flagellin export in the absence of FliS chaperone;Molecular Microbiology;2016-08-02

5. Rearrangements of α-helical structures of FlgN chaperone control the binding affinity for its cognate substrates during flagellar type III export;Molecular Microbiology;2016-06-03

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