ArticleBiochimica et biophysica acta2009
Functional connection between histone acetyltransferase Gcn5p and methyltransferase Hmt1p.
Article in Biochimica et biophysica acta, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 13 citations in OpenAlex.
- Mechanisms and Inhibitors of Histone Arginine Methylation.Chemical record (New York, N.Y.) · 2018Review
- Knockout of the Hmt1p Arginine Methyltransferase inMolecular & cellular proteomics : MCP · 2018Article
- N-alpha-terminal acetylation of histone H4 regulates arginine methylation and ribosomal DNA silencing.PLoS genetics · 2013Article
- Recruitment of Rpd3 to the telomere depends on the protein arginine methyltransferase Hmt1.PloS one · 2012Article
- Protein arginine methylation facilitates cotranscriptional recruitment of pre-mRNA splicing factors.Molecular and cellular biology · 2010Article
- Histone modifying proteins Gcn5 and Hda1 affect flocculation in Saccharomyces cerevisiae during high-gravity fermentation.Current genetics · 2010Article
- Rmt1 catalyzes zinc-finger independent arginine methylation of ribosomal protein Rps2 in Saccharomyces cerevisiae.Biochemical and biophysical research communications · 2010Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 2 countries.
Funding
Abstract
Histone acetylation and methylation are linked to a variety of nuclear activities, most notably transcriptional regulation. Both synergistic and antagonistic relationships between these two modifications have been reported in different systems. Here we show that the budding yeast histone H4 arginine 3 (R3) methyltransferase Hmt1p binds acetylated histones H3 and H4, and importantly, that acetylated H4 is a significantly better methylation substrate for Hmt1p. Kinetic studies show that acetylation at any of the four acetylatable lysine residues of histone H4 results in more efficient methylation. Among the four, K8 acetylation imposes the strongest effect on reducing K(M), consistent with the observed acetylation-stimulated interaction. In vivo, hmt1Delta cells rescue the transcriptional defect caused by GCN5 deletion, indicating that one of the functions of Gcn5p is to neutralize the negative effect of Hmt1p. Mutating either K8 or R3 to alanine causes similar growth defects in selective histone and gcn5 mutant background, suggesting that these two residues function in the same pathway for optimal vegetative growth. Together, these results reveal a functional connection between histone acetylation, methylation, and two of the responsible enzymes, Gcn5p and Hmt1p.
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