PMID: 11606187Oct 19, 2001Paper

Domain-domain interactions of HtpG, an Escherichia coli homologue of eukaryotic HSP90 molecular chaperone

European Journal of Biochemistry
Takayuki K NemotoT Gotoh

Abstract

In the present study, we investigated the domain structure and domain-domain interactions of HtpG, an Escherichia coli homologue of eukaryotic HSP90. Limited proteolysis of recombinant HtpG, revealed three major tryptic sites, i.e. Arg7-Gly8, Arg336-Glu337 and Lys552-Leu553, of which the latter two were located at the positions equivalent to the major cleavage sites of human HSP90alpha. A similar pattern was obtained by papain treatment under nondenaturing conditions but not under denaturing conditions. Thus, HtpG consists of three domains, i.e. Domain A, Met1-Arg336; domain B, Glu337-Lys552; and domain C, Leu553-Ser624, as does HSP90. The domains of HtpG were expressed and their interactions were estimated on polyacrylamide gel electrophoresis under nondenaturing conditions. As a result, two kinds of domain-domain interactions were revealed: domain B interaction with domain A of the same polypeptide and domain C of one partner with domain B of the other in the dimer. Domain B could be structurally and functionally divided into two subdomains, the N-terminal two-thirds (subdomain BI) that interacted with domain A and the C-terminal one-third (subdomain BII) that interacted with domain C. The C-terminal two-thirds of domain A, i...Continue Reading

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Citations

Mar 19, 2008·Cell Stress & Chaperones·Takeshi KobayakawaTakayuki K Nemoto
Jan 28, 2006·FEMS Microbiology Reviews·James P BurnieRuth C Matthews
Aug 22, 2002·The Journal of Biological Chemistry·Shawn VogenYair Argon
Feb 4, 2003·Experimental Biology and Medicine·William B Pratt, David O Toft

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