Deletion analysis of the C-terminal region of a molecular chaperone DnaK from Bacillus licheniformis-Reference-Cited by-同舟云学术

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Deletion analysis of the C-terminal region of a molecular chaperone DnaK from Bacillus licheniformis

Published:2009-05-20 Issue:7 Volume:191 Page:583-593
ISSN:0302-8933
Container-title:Archives of Microbiology
language:en
Short-container-title:Arch Microbiol

Author:

Liang Wan-Chi,Lin Min-Guan,Chi Meng-Chun,Hu Hui-Yu,Lo Huei-Fen,Chang Hui-Ping,Lin Long-Liu

Publisher

Springer Science and Business Media LLC

Subject

Genetics,Molecular Biology,General Medicine,Biochemistry,Microbiology

Link

http://link.springer.com/content/pdf/10.1007/s00203-009-0485-8.pdf

Reference47 articles.

1. Altschul SF, Gish W, Miller W, Myers EW, Lipman DJ (1990) Basic local alignment search tool. J Mol Biol 215:403–410

2. Banecki B, Zylicz M, Bertoli E, Tanfani F (1992) Structural and functional relationships in DnaK and DnaK756 heat-shock proteins from Escherichia coli. J Biol Chem 267:25051–25058

3. Borges JC, Ramos CHI (2006) Spectroscopic and thermodynamic measurements of nucleotide-induced changes in the human 70-kDa heat shock cognate protein. Arch Biochem Biophys 452:46–54

4. Boshoff A, Hennessy F, Blatch GL (2004) The in vivo and in vitro characterization of DnaK from Agrobacterium tumefaciens RUOR. Protein Expr Purif 38:161–169

5. Buchberger A, Theyssen H, Schröder H, McCarty JS, Virgallita G, Milkereit P, Reinstein J, Bukau B (1995) Nucleotide–induced conformational changes in the ATPase and substrate binding domains of the DnaK chaperone provide evidence for interdomain communication. J Biol Chem 270:16903–16910

Cited by 8 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. Molecular cloning, expression, and functional characterization of 70-kDa heat shock protein, DnaK, from Bacillus halodurans;International Journal of Biological Macromolecules;2019-09

2. Gene expression and molecular characterization of a chaperone protein HtpG from Bacillus licheniformis;International Journal of Biological Macromolecules;2016-04

3. Residues Phe103 and Phe149 are critical for the co-chaperone activity of Bacillus licheniformis GrpE;International Journal of Biological Macromolecules;2015-01

4. Introduction of a unique tryptophan residue into various positions of Bacillus licheniformis DnaK;International Journal of Biological Macromolecules;2013-01

5. Fine Tuning of a Biological Machine: DnaK Gains Improved Chaperone Activity by Altered Allosteric Communication and Substrate Binding;ChemBioChem;2011-06-08

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