PDZ-LIKE DOMAINS MEDIATE BINDING-SPECIFICITY IN THE CLP HSP100 FAMILYOF CHAPERONES AND PROTEASE REGULATORY SUBUNITS/

Citation
I. Levchenko et al., PDZ-LIKE DOMAINS MEDIATE BINDING-SPECIFICITY IN THE CLP HSP100 FAMILYOF CHAPERONES AND PROTEASE REGULATORY SUBUNITS/, Cell, 91(7), 1997, pp. 939-947
Citations number
47
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Biology,"Cell Biology
Journal title
CellACNP
ISSN journal
0092-8674
Volume
91
Issue
7
Year of publication
1997
Pages
939 - 947
Database
ISI
SICI code
0092-8674(1997)91:7<939:PDMBIT>2.0.ZU;2-L
Abstract
ClpX, a molecular chaperone and the regulatory subunit of the ClpXP pr otease, is shown to contain tandem modular domains that bind to the C- terminal sequences of target proteins in a manner that parallels funct ional specificity Nuclear magnetic resonance studies show that these C -terminal sequences are displayed as disordered peptides on the surfac e of otherwise folded proteins. The ClpX substrate-binding domains are homologous to sequences in other Clp/Hsp100 proteins and are related more distantly to PDZ domains, which also mediate C-terminal specific protein-protein interactions. Conservation of these binding domains in dicates that the mode of substrate recognition characterized here for ClpX will be a conserved feature among Clp/Hsp100 family members and a distinguishing characteristic between this chaperone family and the H sp70 chaperones.