Set2-catalyzed methylation of histone H3 represses basal expression of GAL4 in Saccharomyces cerevisiae

Landry, J., Sutton, A., Hesman, T., Min, J. R., Xu, R. M., Johnston, M., Sternglanz, R. (September 2003) Set2-catalyzed methylation of histone H3 represses basal expression of GAL4 in Saccharomyces cerevisiae. Molecular and Cellular Biology, 23 (17). pp. 5972-5978. ISSN 0270-7306

URL: http://www.ncbi.nlm.nih.gov/pubmed/12917322
DOI: 10.1128/​MCB.23.17.5972-5978.2003

Abstract

Recent work has shown that histone methylation is an important regulator of transcription. While much is known about the roles of histone methyltransferases (HMTs) in the establishment of heterochromatin, little is known of their roles in the regulation of actively transcribed genes. We describe an in vivo role of the Saccharomyces cerevisiae HMT, Set2. We identified SET2 as a gene necessary for repression of GAL4 basal expression and show that the evolutionarily conserved SACI, SACII, and SET domains of Set2 are necessary for this repression. We confirm that Set2 catalyzes methylation of lysine 36 on the N-terminal tail of histone H3. Conversion of lysine 36 to an unmethylatable arginine causes a decrease in the repression of GAL4 transcription, as does a Deltaset2 mutation. We further show that lysine 36 of histone H3 at GAL4 is methylated and that this methylation is dependent upon the presence of SET2.

Item Type: Paper
Uncontrolled Keywords: RNA-POLYMERASE-II SET DOMAIN LYSINE METHYLTRANSFERASE TRANSCRIPTION PROTEINS GENE CHROMATIN COMPLEX SITE HETEROCHROMATIN
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > histone
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein methylation > histone methylation
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein methylation
organism description > yeast
CSHL Authors:
Communities: CSHL labs > Xu lab
Depositing User: Matt Covey
Date: September 2003
Date Deposited: 10 Jun 2013 14:31
Last Modified: 10 Jun 2013 14:31
PMCID: PMC180946
Related URLs:
URI: http://repository.cshl.edu/id/eprint/27974

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