The effect of co-overproduction of DnaK/DnaJ/GrpE and ClpB proteins on the removal of heat-aggregated proteins from Escherichia coliÎclpB mutant cells â new insight into the role of Hsp70 in a functional cooperation with Hsp100-Reference-Cited by-同舟云学术

The effect of co-overproduction of DnaK/DnaJ/GrpE and ClpB proteins on the removal of heat-aggregated proteins from Escherichia coliÎclpB mutant cells â new insight into the role of Hsp70 in a functional cooperation with Hsp100

Published:2001-11 Issue:2 Volume:204 Page:355-360
ISSN:0378-1097
Container-title:FEMS Microbiology Letters
language:en
Short-container-title:

Author:

Kedzierska Sabina,Matuszewska Ewelina

Publisher

Oxford University Press (OUP)

Subject

Genetics,Molecular Biology,Microbiology

Link

http://academic.oup.com/femsle/article-pdf/204/2/355/19111469/204-2-355.pdf

Reference22 articles.

1. Response of Escherichia coli cell membranes to induction of Î»cI857 prophage by heat shock;Kucharczyk;Mol. Microbiol.,1991

2. The heat shock response of Escherichia coli;ArsÃ©ne;Int. J. Food Microbiol.,2000

3. Heat-inactivated proteins are rescued by the DnaKJ-GrpE set and ClpB chaperones;Motohashi;Proc. Natl. Acad. Sci. USA,1999

4. ClpB cooperates with Dank, DnaJ, and GrpE in suppressing protein aggregation;Zolkiewski;J. Biol. Chem.,1999

5. Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network;Goloubinoff;Proc. Natl. Acad. Sci. USA,1999

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