Linked Life Data

20811616

Source:http://linkedlifedata.com/resource/pubmed/id/20811616

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2010-9-2
pubmed:abstractText
In eukarya and bacteria, lysine methylation is relatively rare and is catalysed by sequence-specific lysine methyltransferases that typically have only a single-protein target. Using RNA polymerase purified from the thermophilic crenarchaeum Sulfolobus solfataricus, we identified 21 methyllysines distributed across 9 subunits of the enzyme. The modified lysines were predominantly in alpha-helices and showed no conserved sequence context. A limited survey of the Thermoproteus tenax proteome revealed widespread modification with 52 methyllysines in 30 different proteins. These observations suggest the presence of an unusual lysine methyltransferase with relaxed specificity in the crenarchaea. Since lysine methylation is known to enhance protein thermostability, this may be an adaptation to a thermophilic lifestyle. The implications of this modification for studies and applications of recombinant crenarchaeal enzymes are discussed.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1472-3654
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
2010
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Extensive lysine methylation in hyperthermophilic crenarchaea: potential implications for protein stability and recombinant enzymes.
pubmed:affiliation
Centre for Biomolecular Sciences, University of St Andrews, Fife KY16 9ST, UK. cb2@st-and.ac.uk
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't