Linked Life Data

8055955

Source:http://linkedlifedata.com/resource/pubmed/id/8055955

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1994-9-15
pubmed:abstractText
Low amounts of Semliki Forest virus capsid protein transferred into target cells by electroporation-mediated delivery (10(3)-10(4) molecules incorporated/cell) confer thermal resistance resulting in enhanced survival. Furthermore, when exposed to 43 degrees C, these cells display an enhanced expression of heat-shock protein-70 and a translational thermotolerance. Similarly, low amounts of capsid protein transferred into cells in which transcription is blocked by actinomycin D, also protect the translational machinery at 43 degrees C. In a cell-free translation system, added capsid protein appears to modulate translational efficiency of endogenous mRNAs. At approximately 1 molecule/ribosome, capsid protein is able to enhance translation at 30 degrees C and at 43 degrees C. In contrast, high concentrations of capsid protein are responsible for a marked inhibition of protein synthesis at 30 degrees C, but only hamper translational thermotolerance at 43 degrees C. Our results favor the hypothesis that small amounts of capsid protein trigger a chaperone-like activity that is able to protect the translational machinery from thermal damage.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
223
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
791-7
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Modulation of thermoprotection and translational thermotolerance induced by Semliki Forest virus capsid protein.
pubmed:affiliation
Institute of Medical Microbiology, University of Berne, Switzerland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't