| pubmed-article:16426232 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16426232 | lifeskim:mentions | umls-concept:C0043393 | lld:lifeskim |
| pubmed-article:16426232 | lifeskim:mentions | umls-concept:C0040113 | lld:lifeskim |
| pubmed-article:16426232 | lifeskim:mentions | umls-concept:C0230445 | lld:lifeskim |
| pubmed-article:16426232 | lifeskim:mentions | umls-concept:C0019652 | lld:lifeskim |
| pubmed-article:16426232 | lifeskim:mentions | umls-concept:C0019646 | lld:lifeskim |
| pubmed-article:16426232 | lifeskim:mentions | umls-concept:C1883254 | lld:lifeskim |
| pubmed-article:16426232 | lifeskim:mentions | umls-concept:C0007382 | lld:lifeskim |
| pubmed-article:16426232 | lifeskim:mentions | umls-concept:C1533691 | lld:lifeskim |
| pubmed-article:16426232 | lifeskim:mentions | umls-concept:C1522492 | lld:lifeskim |
| pubmed-article:16426232 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:16426232 | pubmed:dateCreated | 2006-4-6 | lld:pubmed |
| pubmed-article:16426232 | pubmed:abstractText | The HSL7 (histone synthetic lethal 7) gene in the yeast Saccharomyces cerevisiae encodes a protein with close sequence similarity to the mammalian PRMT5 protein, a member of the class of protein arginine methyltransferases that catalyses the formation of omega-N(G)-monomethylarginine and symmetric omega-N(G),N'(G)-dimethylarginine residues in a number of methyl-accepting species. A full-length HSL7 construct was expressed as a FLAG-tagged protein in Saccharomyces cerevisiae. We found that FLAG-tagged Hsl7 effectively catalyses the transfer of methyl groups from S-adenosyl-[methyl-3H]-L-methionine to calf thymus histone H2A. When the acid-hydrolysed radiolabelled protein products were separated by high-resolution cation-exchange chromatography, we were able to detect one tritiated species that co-migrated with an omega-N(G)-monomethylarginine standard. No radioactivity was observed that co-migrated with either the asymmetric or symmetric dimethylated derivatives. In control experiments, no methylation of histone H2A was found with two mutant constructs of Hsl7. Surprisingly, FLAG-Hsl7 does not appear to effectively catalyse the in vitro methylation of a GST (glutathione S-transferase)-GAR [glycine- and arginine-rich human fibrillarin-(1-148) peptide] fusion protein or bovine brain myelin basic protein, both good methyl-accepting substrates for the human homologue PRMT5. Additionally, FLAG-Hsl7 demonstrates no activity on purified calf thymus histones H1, H2B, H3 or H4. GST-Rmt1, the GST-fusion protein of the major yeast protein arginine methyltransferase, was also found to methylate calf thymus histone H2A. Although we detected Rmt1-dependent arginine methylation in vivo in purified yeast histones H2A, H2B, H3 and H4, we found no evidence for Hsl7-dependent methylation of endogenous yeast histones. The physiological substrates of the Hsl7 enzyme remain to be identified. | lld:pubmed |
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| pubmed-article:16426232 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:16426232 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:16426232 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16426232 | pubmed:month | May | lld:pubmed |
| pubmed-article:16426232 | pubmed:issn | 1470-8728 | lld:pubmed |
| pubmed-article:16426232 | pubmed:author | pubmed-author:ClarkeStevenS | lld:pubmed |
| pubmed-article:16426232 | pubmed:author | pubmed-author:FrankelAdamA | lld:pubmed |
| pubmed-article:16426232 | pubmed:author | pubmed-author:KatzJonathan... | lld:pubmed |
| pubmed-article:16426232 | pubmed:author | pubmed-author:MirandaTina... | lld:pubmed |
| pubmed-article:16426232 | pubmed:author | pubmed-author:MirandaMarkM | lld:pubmed |
| pubmed-article:16426232 | pubmed:author | pubmed-author:SayeghJoyceJ | lld:pubmed |
| pubmed-article:16426232 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:16426232 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:16426232 | pubmed:volume | 395 | lld:pubmed |
| pubmed-article:16426232 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16426232 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16426232 | pubmed:pagination | 563-70 | lld:pubmed |
| pubmed-article:16426232 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:16426232 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16426232 | pubmed:articleTitle | Yeast Hsl7 (histone synthetic lethal 7) catalyses the in vitro formation of omega-N(G)-monomethylarginine in calf thymus histone H2A. | lld:pubmed |
| pubmed-article:16426232 | pubmed:affiliation | The Department of Chemistry and Biochemistry and the Molecular Biology Institute, UCLA (University of California, Los Angeles), Los Angeles, CA 90095-1569, USA. | lld:pubmed |
| pubmed-article:16426232 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16426232 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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