Linked Life Data

15498567

Source:http://linkedlifedata.com/resource/pubmed/id/15498567

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2004-10-22
pubmed:abstractText
Here, we produced the C-terminal truncation variants of mouse inducible heat shock protein 72 (Hsp72) to elucidate the regulatory role of the C-terminal helical lid of Hsp70 for substrate recognition. All of the truncation variants containing the substrate binding domain bound a short-length peptide substrate CLLLSAPRR. When a large mass reduced carboxymethyl alpha-lactalbumin (RCMLA) as a substrate was used in gel filtration experiment, we observed the complex formation only for the truncation variants containing the long alpha-helix C in the helical lid. However, RCMLA binding occurred even for the variants lacking alpha-helix C when their C-terminal region was anchored onto a solid phase. Together with the finding that helix C is involved in the self-association of Hsp70, our present data suggest that the C-terminal region of Hsp70 modulates the substrate recognition and its kinetics may be substrate-mass dependent.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
576
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
381-6
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Role of the C-terminal region of mouse inducible Hsp72 in the recognition of peptide substrate for chaperone activity.
pubmed:affiliation
Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Goka-sho, Uji, Kyoto 611-0011, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't