Linked Life Data

9873020

Source:http://linkedlifedata.com/resource/pubmed/id/9873020

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1999-2-5
pubmed:abstractText
We used sequence motifs conserved in S-adenosylmethionine-dependent methyltransferases to identify 26 putative methyltransferases from the complete genome of the yeast Saccharomyces cerevisiae. Seven sequences with the best matches to the methyltransferase consensus motifs were selected for further study. We prepared yeast disruption mutants of each of the genes encoding these sequences, and we found that disruption of the YJL125c gene is lethal, whereas disruptions of YCR047c and YDR140w lead to slow growth phenotypes. Normal growth was observed when the YDL201w, YDR465c, YHR209w, and YOR240w genes were disrupted. Initial analysis of protein methylation patterns of all mutants by amino acid analysis revealed that the YDR465c mutant has a defect in the methylation of the delta-nitrogen atom of arginine residues. We propose that YDR465c codes for the methyltransferase responsible for this recently characterized type of protein methylation, and we designate the enzyme as Rmt2 (protein arginine methyltransferase). In addition, we show that the methylation of susceptible residues in Rmt2 substrates is likely to take place on nascent polypeptide chains and that these substrates exist in the cell as fully methylated species. Interestingly, Rmt2 has 27% sequence identity over 138 amino acids to the mammalian guanidinoacetate N-methyltransferase, an enzyme responsible for methylating the delta-nitrogen of the small molecule guanidinoacetate.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
8
pubmed:volume
274
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
814-24
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
S-Adenosylmethionine-dependent methylation in Saccharomyces cerevisiae. Identification of a novel protein arginine methyltransferase.
pubmed:affiliation
Department of Chemistry and Biochemistry and the Molecular Biology Institute, University of California, Los Angeles, California 90095-1569, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.