Linked Life Data

14501945

Source:http://linkedlifedata.com/resource/pubmed/id/14501945

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2003-9-22
pubmed:abstractText
The expression of heat shock or stress proteins (hsps) is a widespread response to stress that results in the protection of cells from subsequent insults, coined stress tolerance. Stress tolerance is apparently due to the preservation of several cellular structures and processes, such as translation. Protection of protein synthesis has been correlated with the presence of Hsp70. In the present study, Hsp70 was found to interact with translating ribosomes. This interaction is due to the preferential binding of Hsp70 to the 40S ribosomal subunit. Additionally, Hsp70 seems to interact weakly with nascent polypeptides within the 60S subunit. The interaction between Hsp70 and ribosomal subunits could also be observed in vitro conditions. Binding of Hsp70 to ribosomes was salt resistant, suggesting that this protein is not bound to transiently associated translational factors. Moreover, protection of protein synthesis requires new gene expression. We speculate that the binding of Hsp70 to ribosomes is part of a mechanism to guarantee the rapid and abundant protein synthesis during stress, particularly the translation of mRNAs encoding for hsps.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1073-2322
pubmed:author
pubmed:issnType
Print
pubmed:volume
20
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
320-5
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
HSP70 interacts with ribosomal subunits of thermotolerant cells.
pubmed:affiliation
Department of Physiology, Johns Hopkins Medical School, Baltimore, Maryland 21205, USA.
pubmed:publicationType
Journal Article, In Vitro, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't