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PMID: 11440840 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Chromatin silencing protein and pachytene checkpoint regulator Dot1p has a methyltransferase fold.

Trends in biochemical sciences ·Vol. 26 ·No. 7 ·2001-07-00 ·Pages 405-7

Dlakić M

Abstract

Although protein methylation has been observed for decades, its functional significance has remained largely unclear. Using sensitive profile searches and structural modeling, chromatin silencing protein and meiotic recombination checkpoint regulator Dot1p was identified as a putative protein methyltransferase. Along with recent results that link histone H3 methylation with chromatin silencing, this finding suggests that an expanded combinatorial repertoire of protein modifications affects transcriptional regulation.

MeSH Terms
Amino Acid Sequence Animals Chromatin/chemistry,metabolism DNA Methylation Histone-Lysine N-Methyltransferase Histones Humans Methylation Methyltransferases/chemistry Models, Molecular Molecular Sequence Data Nuclear Proteins/chemistry Protein Folding Saccharomyces cerevisiae Proteins Sequence Homology, Amino Acid Transcription, Genetic
Chemicals
Chromatin Histones Nuclear Proteins Saccharomyces cerevisiae Proteins Methyltransferases Dot1 protein, S cerevisiae Histone-Lysine N-Methyltransferase
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Dlakić M
Dept of Biological Chemistry, The University of Michigan Medical School, 48109-0606, Ann Arbor, MI, USA. mensur@umich.edu
Article Info
Journal
Trends in biochemical sciences
Abbr.
Trends Biochem Sci
ISSN
0968-0004
Published
2001-07-00
Pages
405-7
Language
English
Region
England
NLM ID
7610674
Subset
IM
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