|PROSITE documentation PDOC00270 [for PROSITE entry PS00298]|
Prokaryotic and eukaryotic organisms respond to heat shock or other environmental stress by the induction of the synthesis of proteins collectively known as heat-shock proteins (hsp) . Amongst them is a family of proteins, with an average molecular weight of 90 Kd, known as the hsp90 proteins. Proteins known to belong to this family are:
The exact function of hsp90 proteins is not yet known. In higher eukaryotes, hsp90 has been found associated with steroid hormone receptors, with tyrosine kinase oncogene products of several retroviruses, with eIF2α kinase, and with actin and tubulin. Hsp90 are probable chaperonins that possess ATPase activity [2,3].
As a signature pattern for the hsp90 family of proteins, we have selected a highly conserved region found in the N-terminal part of these proteins.Last update:
April 2006 / Pattern revised.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Lindquist S. Craig E.A.|
|Title||The heat-shock proteins.|
|Source||Annu. Rev. Genet. 22:631-677(1988).|
|2||Authors||Nadeau K. Das A. Walsh C.T.|
|Title||Hsp90 chaperonins possess ATPase activity and bind heat shock transcription factors and peptidyl prolyl isomerases.|
|Source||J. Biol. Chem. 268:1479-1487(1993).|
|3||Authors||Jakob U. Buchner J.|
|Title||Assisting spontaneity: the role of Hsp90 and small Hsps as molecular chaperones.|
|Source||Trends Biochem. Sci. 19:205-211(1994).|