HDA2 and HDA3 are related proteins that interact with and are essential for the activity of the yeast histone deacetylase HDA1

Wu, J. S., Carman, A. A., Kobayashi, R., Suka, N., Grunstein, M. (April 2001) HDA2 and HDA3 are related proteins that interact with and are essential for the activity of the yeast histone deacetylase HDA1. Proceedings of the National Academy of Sciences of the United States of America, 98 (8). pp. 4391-4396. ISSN 0027-8424

URL: http://www.ncbi.nlm.nih.gov/pubmed/11287668
DOI: 10.1073/pnas.081560698

Abstract

Histone deacetylase HDA1, the prototype for the class II mammalian deacetylases, is likely the catalytic subunit of the HDA1-containing complex that is involved in TUP1-specific repression and global deacetylation in yeast. Although the class I RPD3-like enzymatic complexes have been well characterized, little is known about the identity and interactions of the factors that associate to form the HDA1 complex. In this paper, we identify related HDA2 and HDA3 proteins that are found in the HDA1 complex and show that HDA1 interacts with itself and with the HDA2-HDA3 subcomplex to form a likely tetramer. These interactions are necessary for catalytic activity because mutations in any of the three components disrupt activity both in vitro and in vivo. In this respect the HDA1 complex differs from yeast RPD3, which has components such as SIN3 that are not essential for activity in vitro, and yeast HOS3, which has intrinsic in vitro activity as a homodimer in the absence of other subunits.

Item Type: Paper
Uncontrolled Keywords: TRANSCRIPTIONAL REPRESSION SACCHAROMYCES-CEREVISIAE COMPLEX RECRUITMENT RPD3 H4 HETEROCHROMATIN DOMAIN SIR3 UME6
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing
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 > enzymes > histone deacetylase
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein methylation
organism description > yeast
CSHL Authors:
Communities: CSHL labs > Kobayashi lab
Depositing User: Matt Covey
Date: April 2001
Date Deposited: 15 Jan 2014 20:07
Last Modified: 15 Jan 2014 20:07
PMCID: PMC31845
Related URLs:
URI: http://repository.cshl.edu/id/eprint/29330

Actions (login required)

Administrator's edit/view item Administrator's edit/view item
CSHL HomeAbout CSHLResearchEducationNews & FeaturesCampus & Public EventsCareersGiving