Asf1 Can Promote Trimethylation of H3 K36 by Set2

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Published inMolecular and Cellular Biology Vol. 30; no. 5; pp. 1116 - 1129
Main Authors Lin, Ling-ju, Minard, Laura V., Johnston, Gerald C., Singer, Richard A., Schultz, Michael C.
Format Journal Article
LanguageEnglish
Published United States American Society for Microbiology 01.03.2010
Taylor & Francis
American Society for Microbiology (ASM)
Subjects
Cell Cycle
Cell Cycle Proteins - genetics
Cell Cycle Proteins - metabolism
Chromatin - genetics
Chromatin - metabolism
DNA Damage
DNA, Fungal - genetics
DNA, Fungal - metabolism
Gene Deletion
Gene Regulatory Networks
Genes, Fungal
Histones - chemistry
Histones - metabolism
Methylation
Methyltransferases - genetics
Methyltransferases - metabolism
Models, Biological
Molecular Chaperones - genetics
Molecular Chaperones - metabolism
Saccharomyces cerevisiae - cytology
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins - genetics
Saccharomyces cerevisiae Proteins - metabolism
Transcription, Genetic
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Asf1 is a conserved histone H3/H4 chaperone that can assemble and disassemble nucleosomes and promote histone acetylation. Set2 is an H3 K36 methyltransferase. The functions of these proteins intersect in the context of transcription elongation by RNA polymerase II: both contribute to the establishment of repressive chromatin structures that inhibit spurious intragenic transcription. Here we characterize further interactions between budding yeast ( Saccharomyces cerevisiae ) Asf1 and Set2 using assays of intragenic transcription, H3/H4 posttranslational modification, coding region cross-linking of Asf1 and Set2, and cooccurrence of Asf1 and Set2 in protein complexes. We find that at some genes Asf1 and Set2 control chromatin metabolism as components of separate pathways. However, the existence of a low-abundance complex containing both proteins suggests that Asf1 and Set2 can more directly collaborate in chromatin regulation. Consistent with this possibility, we show that Asf1 stimulates Set2 occupancy of the coding region of a highly transcribed gene by a mechanism that depends on Asf1 binding to H3/H4. This function of Asf1 promotes the switch from di- to trimethylation of H3 K36 at that gene. These results support the view that Set2 function in chromatin metabolism can intimately involve histone chaperone Asf1.
Asf1 is a conserved histone H3/H4 chaperone that can assemble and disassemble nucleosomes and promote histone acetylation. Set2 is an H3 K36 methyltransferase. The functions of these proteins intersect in the context of transcription elongation by RNA polymerase II: both contribute to the establishment of repressive chromatin structures that inhibit spurious intragenic transcription. Here we characterize further interactions between budding yeast (Saccharomyces cerevisiae) Asf1 and Set2 using assays of intragenic transcription, H3/H4 posttranslational modification, coding region cross-linking of Asf1 and Set2, and cooccurrence of Asf1 and Set2 in protein complexes. We find that at some genes Asf1 and Set2 control chromatin metabolism as components of separate pathways. However, the existence of a low-abundance complex containing both proteins suggests that Asf1 and Set2 can more directly collaborate in chromatin regulation. Consistent with this possibility, we show that Asf1 stimulates Set2 occupancy of the coding region of a highly transcribed gene by a mechanism that depends on Asf1 binding to H3/H4. This function of Asf1 promotes the switch from di- to trimethylation of H3 K36 at that gene. These results support the view that Set2 function in chromatin metabolism can intimately involve histone chaperone Asf1.
Author Michael C. Schultz
Laura V. Minard
Ling-ju Lin
Gerald C. Johnston
Richard A. Singer
AuthorAffiliation Department of Biochemistry, University of Alberta, Edmonton, Alberta, Canada T6G 2H7, 1 Department of Microbiology and Immunology, 2 Department of Biochemistry and Molecular Biology, Dalhousie University, Halifax, Nova Scotia, Canada B3H 1X5 3
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Snippet Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley...
Asf1 is a conserved histone H3/H4 chaperone that can assemble and disassemble nucleosomes and promote histone acetylation. Set2 is an H3 K36 methyltransferase....
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SubjectTerms Cell Cycle
Cell Cycle Proteins - genetics
Cell Cycle Proteins - metabolism
Chromatin - genetics
Chromatin - metabolism
DNA Damage
DNA, Fungal - genetics
DNA, Fungal - metabolism
Gene Deletion
Gene Regulatory Networks
Genes, Fungal
Histones - chemistry
Histones - metabolism
Methylation
Methyltransferases - genetics
Methyltransferases - metabolism
Models, Biological
Molecular Chaperones - genetics
Molecular Chaperones - metabolism
Saccharomyces cerevisiae - cytology
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins - genetics
Saccharomyces cerevisiae Proteins - metabolism
Transcription, Genetic
Title Asf1 Can Promote Trimethylation of H3 K36 by Set2
URI http://mcb.asm.org/content/30/5/1116.abstract
https://www.tandfonline.com/doi/abs/10.1128/MCB.01229-09
https://www.ncbi.nlm.nih.gov/pubmed/20048053
https://pubmed.ncbi.nlm.nih.gov/PMC2820888
Volume 30
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