Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2008-2-4
pubmed:abstractText
Eukaryotic cytosolic seryl-tRNA synthetases (SerRS) have idiosyncratic C-terminal extensions not present in prokaryotic counterparts. The extensions of two eukaryotic SerRSs were subjected to mutagenesis and partial truncation. Only minor parts of the yeast or maize SerRS extensions, adjacent to the catalytic core (7 of 20 and 8 of 26 amino acids, respectively), were found to be indispensable for protein stability. Truncated proteins with substantially shortened extensions displayed unaltered catalytic properties and could complement a Saccharomyces cerevisiae strain with a disrupted SerRS gene, if these proximal regions were left intact. Although the yeast C-terminal SerRS extension is required for Pex21p binding, the maize counterpart with an appended yeast SerRS extension remained incapable of Pex21p binding, implying that additional regions of yeast SerRS may also contribute to the interaction with the peroxin. The proximal region of the eukaryotic SerRS C-terminal extension is indispensable for protein stability, while the remaining part of the extension remains available for other functions, such as species-specific protein:protein interactions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1096-0384
pubmed:author
pubmed:issnType
Electronic
pubmed:day
15
pubmed:volume
470
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
129-38
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
The proximal region of a noncatalytic eukaryotic seryl-tRNA synthetase extension is required for protein stability in vitro and in vivo.
pubmed:affiliation
Department of Chemistry, Faculty of Science, University of Zagreb, Horvatovac 102a, 10000 Zagreb, Croatia.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't