Hsp90 chaperonins possess ATPase activity and bind heat shock transcription factors and peptidyl prolyl isomerases
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 …
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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117400
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