Chromatin silencing protein and pachytene checkpoint regulator Dot1p has a methyltransferase fold.
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.
Dlakić
M
M
Dept of Biological Chemistry, The University of Michigan Medical School, 48109-0606, Ann Arbor, MI, USA. mensur@umich.edu
D000595:Amino Acid Sequence; D000818:Animals; D002843:Chromatin / Q000737:chemistry / Q000378:metabolism*; D019175:DNA Methylation; D011495:Histone-Lysine N-Methyltransferase; D006657:Histones; D006801:Humans; D008745:Methylation; D008780:Methyltransferases / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009687:Nuclear Proteins / Q000737:chemistry*; D017510:Protein Folding; D029701:Saccharomyces cerevisiae Proteins; D017386:Sequence Homology, Amino Acid; D014158:Transcription, Genetic
D002843:Chromatin; D006657:Histones; D009687:Nuclear Proteins; D029701:Saccharomyces cerevisiae Proteins; D008780:Methyltransferases; C416235:Dot1 protein, S cerevisiae; D011495:Histone-Lysine N-Methyltransferase