Identification of a transcriptional repressor related to the noncatalytic domain of histone deacetylases 4 and 5

Histone deacetylases (HDACs) are involved in regulating transcription by modifying the core histones of the nucleosome. To date, six HDACs have been identified in mammalian cells: the yeast RPD3 homologs HDAC1, 2, and 3 and the yeast HDA1 homologs HDAC4, 5, and 6. HDAC4 and HDAC5 contain a noncataly...

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Main Authors: Zhou, Xianbo, Richon, Victoria M., Rifkind, Richard A., Marks, Paul A.
Formato: Artigo
Idioma:en
Publicado em: The National Academy of Sciences 2000
Assuntos:
Biological Sciences
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC15519/
https://ncbi.nlm.nih.gov/pubmed/10655483
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spelling pubmed-155192001-03-07 Identification of a transcriptional repressor related to the noncatalytic domain of histone deacetylases 4 and 5 Zhou, Xianbo Richon, Victoria M. Rifkind, Richard A. Marks, Paul A. Proc Natl Acad Sci U S A Biological Sciences Histone deacetylases (HDACs) are involved in regulating transcription by modifying the core histones of the nucleosome. To date, six HDACs have been identified in mammalian cells: the yeast RPD3 homologs HDAC1, 2, and 3 and the yeast HDA1 homologs HDAC4, 5, and 6. HDAC4 and HDAC5 contain a noncatalytic N-terminal domain. Herein, we report the identification of a protein HDRP (HDAC-related protein) that shares 50% identity in deduced amino acid sequence to the noncatalytic N-terminal domain of HDAC4 and 5. The steady-state levels of HDRP mRNA are high in human brain, heart, and skeletal muscle and low in the several other tissues. HDRP has an apparent molecular mass of approximately 75 kDa. HDRP does not possess intrinsic HDAC activity but forms complexes with both HDAC1 and HDAC3. HDRP represses both basal and activated transcription in transient transfection assays when tethered to DNA as a Gal4-fusion protein. HDAC inhibitors do not reverse transcriptional repression mediated by Gal4–HDRP. Thus, HDRP is a transcriptional repressor and can repress transcription in the presence of HDAC inhibitors. The National Academy of Sciences 2000-02-01 /pmc/articles/PMC15519/ /pubmed/10655483 Text en Copyright © 2000, The National Academy of Sciences
institution US National Library of Medicine
collection PubMed Central
language en
format Article
topic Biological Sciences
spellingShingle Biological Sciences
Zhou, Xianbo
Richon, Victoria M.
Rifkind, Richard A.
Marks, Paul A.
Identification of a transcriptional repressor related to the noncatalytic domain of histone deacetylases 4 and 5
description Histone deacetylases (HDACs) are involved in regulating transcription by modifying the core histones of the nucleosome. To date, six HDACs have been identified in mammalian cells: the yeast RPD3 homologs HDAC1, 2, and 3 and the yeast HDA1 homologs HDAC4, 5, and 6. HDAC4 and HDAC5 contain a noncatalytic N-terminal domain. Herein, we report the identification of a protein HDRP (HDAC-related protein) that shares 50% identity in deduced amino acid sequence to the noncatalytic N-terminal domain of HDAC4 and 5. The steady-state levels of HDRP mRNA are high in human brain, heart, and skeletal muscle and low in the several other tissues. HDRP has an apparent molecular mass of approximately 75 kDa. HDRP does not possess intrinsic HDAC activity but forms complexes with both HDAC1 and HDAC3. HDRP represses both basal and activated transcription in transient transfection assays when tethered to DNA as a Gal4-fusion protein. HDAC inhibitors do not reverse transcriptional repression mediated by Gal4–HDRP. Thus, HDRP is a transcriptional repressor and can repress transcription in the presence of HDAC inhibitors.
author Zhou, Xianbo
Richon, Victoria M.
Rifkind, Richard A.
Marks, Paul A.
author_facet Zhou, Xianbo
Richon, Victoria M.
Rifkind, Richard A.
Marks, Paul A.
author_sort Zhou, Xianbo
title Identification of a transcriptional repressor related to the noncatalytic domain of histone deacetylases 4 and 5
title_short Identification of a transcriptional repressor related to the noncatalytic domain of histone deacetylases 4 and 5
title_full Identification of a transcriptional repressor related to the noncatalytic domain of histone deacetylases 4 and 5
title_fullStr Identification of a transcriptional repressor related to the noncatalytic domain of histone deacetylases 4 and 5
title_full_unstemmed Identification of a transcriptional repressor related to the noncatalytic domain of histone deacetylases 4 and 5
title_sort identification of a transcriptional repressor related to the noncatalytic domain of histone deacetylases 4 and 5
publisher The National Academy of Sciences
publisher_facet The National Academy of Sciences
publishDate 2000
url https://ncbi.nlm.nih.gov/pmc/articles/PMC15519/
https://ncbi.nlm.nih.gov/pubmed/10655483
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