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PMID: 12193658 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Histone H3 lysine 4 methylation is mediated by Set1 and promotes maintenance of active chromatin states in fission yeast.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 99 Suppl 4 ·2002-12-10 ·Pages 16438-45

Noma K, Grewal SI

Abstract

Methylation of histone H3 at lysine 4 (H3 Lys-4) or lysine 9 (H3 Lys-9) is known to define active and silent chromosomal domains respectively from fission yeast to humans. However, in budding yeast, H3 Lys-4 methylation is also necessary for silent chromatin assembly at telomeres and ribosomal DNA. Here we demonstrate that deletion of set1, which encodes a protein containing an RNA recognition motif at its amino terminus and a SET domain at the carboxy terminus, abolishes H3 Lys-4 methylation in fission yeast. Unlike in budding yeast, Set1-mediated H3 Lys-4 methylation is not required for heterochromatin assembly at the silent mating-type region and centromeres in fission yeast. Our analysis suggests that H3 Lys-4 methylation is a stable histone modification present throughout the cell cycle, including mitosis. The loss of H3 Lys-4 methylation in set1Delta cells is correlated with a decrease in histone H3 acetylation levels, suggesting a mechanistic link between H3 Lys-4 methylation and acetylation of the H3 tail. We suggest that methylation of H3 Lys-4 primarily acts in the maintenance of transcriptionally poised euchromatic domains, and that this modification is dispensable for heterochromatin formation in fission yeast, which instead utilizes H3 Lys-9 methylation.

MeSH Terms
Cell Cycle Chromatin/metabolism Fluorescent Antibody Technique Histones/chemistry,metabolism Lysine/metabolism Methylation Schizosaccharomyces/cytology,genetics,metabolism
Chemicals
Chromatin Histones Lysine
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Noma Ken-ichi
Cold Spring Harbor Laboratory, P.O. Box 100, NY 11724, USA.
Grewal Shiv I S
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.182436399
Published
2002-12-10
Epub
2002-00-22
Pages
16438-45
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC139906
Subset
IM
Grants
NIGMS NIH HHS · R01 GM059772 · United States
NIGMS NIH HHS · GM59772 · United States
External Links
PubMed source DOI: 10.1073/pnas.182436399 PMC Full Text View journal details
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