Functionality of Class A and Class B J-protein co-chaperones with Hsp70.
FEBS Lett
; 589(19 Pt B): 2825-30, 2015 Sep 14.
Article
in En
| MEDLINE
| ID: mdl-26247431
ABSTRACT
At their C-termini, cytosolic Hsp70s have an EEVD tetrapeptide that interacts with J-protein co-chaperones of the B, but not A, class. This interaction is required for partnering with yeast B-type J-proteins in protein folding. Here we report conservation of this feature. Human B-type J-proteins also have a stringent EEVD requirement. Human A-type J-proteins function less well than their yeast orthologs with Hsp70ΔEEVD. Changes in the zinc binding domain, a domain absent in B-type J-proteins, overcomes this partial EEVD dependence. Our results suggest that the structurally similar A- and B-class J-proteins of the cytosol have evolved conserved, yet distinct, features that enhance specialized functionality of Hsp70 machinery.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
HSP70 Heat-Shock Proteins
/
HSP40 Heat-Shock Proteins
Limits:
Humans
Language:
En
Journal:
FEBS Lett
Year:
2015
Document type:
Article
Affiliation country:
United States