Linked Life Data

3003072

Source:http://linkedlifedata.com/resource/pubmed/id/3003072

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1986-3-12
pubmed:databankReference
pubmed:abstractText
Unmethylated calmodulins have been enzymatically methylated at lysine 115, and a direct effect of this methylation on NAD kinase activation has been shown. Similar to naturally occurring calmodulins with trimethyllysine 115, the enzymatically methylated calmodulins activated an NAD kinase preparation to a maximal level that was at least 3-fold lower than the level of activation obtained with the corresponding unmethylated calmodulins. Methylation did not alter the cyclic nucleotide phosphodiesterase activator properties of these calmodulins. A genetically engineered calmodulin containing an arginine at position 115 instead of a lysine was produced by site-specific mutagenesis of a cloned synthetic calmodulin gene. The arginine derivative retained the higher maximal NAD kinase activator properties of the unmethylated calmodulins but was no longer susceptible to the effects of the methyltransferase. The data indicate that the reduction in the level of NAD kinase activation is the direct result of trimethylation of lysine 115 of calmodulin, provide a precedent for a functional effect of trimethyllysine in a protein, and raise the possibility that some of calmodulin's physiological activities may be affected by lysine methylation.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
261
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1491-4
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
Trimethyllysine and protein function. Effect of methylation and mutagenesis of lysine 115 of calmodulin on NAD kinase activation.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.