Linked Life Data

10622731

Source:http://linkedlifedata.com/resource/pubmed/id/10622731

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2000-2-2
pubmed:abstractText
To investigate the possible influence of the local rates of translation on protein folding, 16 consecutive rare (in Escherichia coli) codons in the chloramphenicol acetyltransferase (CAT) gene have been replaced by frequent ones. Site-directed silent mutagenesis reduced the pauses in translation of CAT in E. coli S30 extract cell-free system and led to the acceleration of the overall rate of CAT protein synthesis. At the same time, the silently mutated protein (with unaltered protein sequence) synthesized in the E. coli S30 extract system was shown to possess 20% lower specific activity. The data suggest that kinetics of protein translation can affect the in vivo protein-folding pathway, leading to increased levels of protein misfolding.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
462
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
387-91
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Synonymous codon substitutions affect ribosome traffic and protein folding during in vitro translation.
pubmed:affiliation
Centre de Génétique Moléculaire, CNRS, Gif-sur-Yvette, France. anton.komar@cgm.cnrs-gif.fr
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't