Hsp90 chaperonins possess ATPase activity and bind heat shock transcription factors and peptidyl prolyl isomerases

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ID: 117400
1993
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Abstract
Heat shock proteins of the 82-90 kDa class (hsp82 and hsp90) are abundant, conserved, and ubiquitous from prokaryotes to eukaryotes. Although proposed to be chaperones, they had not been reported to possess enzymatic activity until our recent observation that pure trypanosomatid hsp83 had potent ATP …
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Authors Nadeau K;Das A;Walsh CT;;
Journal The Journal of biological chemistry
Year 1993
DOI
DOI not found
URL
https://www.ncbi.nlm.nih.gov/pubmed/8419347
Keywords
National Center for Biotechnology Information NCBI NLM MEDLINE genetic animals humans pubmed abstract nih national institutes of health national library of medicine research support non-u.s. gov't u.s. gov't P.H.S. Rats Transcription Factors / metabolism* Promoter Regions kinetics electrophoresis molecular weight protein binding hot temperature phosphorylation k nadeau pmid:8419347 a das c t walsh adenosine triphosphatases / isolation & purification adenosine triphosphatases / metabolism* amino acid isomerases / metabolism* carrier proteins / metabolism* crithidia fasciculata / metabolism cyclosporins / metabolism polyacrylamide gel escherichia coli / metabolism* heat-shock proteins / metabolism* peptidylprolyl isomerase saccharomyces cerevisiae / metabolism*

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