PMID- 10655483
OWN - NLM
STAT- MEDLINE
DCOM- 20000302
LR  - 20191210
IS  - 0027-8424 (Print)
IS  - 0027-8424 (Linking)
VI  - 97
IP  - 3
DP  - 2000 Feb 1
TI  - Identification of a transcriptional repressor related to the noncatalytic domain 
      of histone deacetylases 4 and 5.
PG  - 1056-61
AB  - 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.
FAU - Zhou, X
AU  - Zhou X
AD  - Cell Biology Program, Sloan-Kettering Institute, Memorial Sloan-Kettering Cancer 
      Center and Graduate School of Medical Sciences, Cornell University Medical
      School, New York, NY 10021, USA.
FAU - Richon, V M
AU  - Richon VM
FAU - Rifkind, R A
AU  - Rifkind RA
FAU - Marks, P A
AU  - Marks PA
LA  - eng
GR  - CA-0974823/CA/NCI NIH HHS/United States
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Proc Natl Acad Sci U S A
JT  - Proceedings of the National Academy of Sciences of the United States of America
JID - 7505876
RN  - 0 (RNA, Messenger)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (Repressor Proteins)
RN  - EC 3.5.1.98 (HDAC1 protein, human)
RN  - EC 3.5.1.98 (HDAC4 protein, human)
RN  - EC 3.5.1.98 (HDAC5 protein, human)
RN  - EC 3.5.1.98 (HDAC9 protein, human)
RN  - EC 3.5.1.98 (Histone Deacetylase 1)
RN  - EC 3.5.1.98 (Histone Deacetylases)
RN  - EC 3.5.1.98 (histone deacetylase 3)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - COS Cells
MH  - Chlorocebus aethiops
MH  - Histone Deacetylase 1
MH  - Histone Deacetylases/*chemistry/metabolism
MH  - Humans
MH  - Molecular Sequence Data
MH  - Organ Specificity
MH  - RNA, Messenger/genetics
MH  - Recombinant Fusion Proteins/chemistry/metabolism
MH  - Repressor Proteins/*chemistry/genetics/*isolation & purification
MH  - Sequence Alignment
MH  - Sequence Homology, Amino Acid
MH  - Transcription, Genetic
MH  - Transfection
PMC - PMC15519
EDAT- 2000/02/03 09:00
MHDA- 2000/03/04 09:00
CRDT- 2000/02/03 09:00
PHST- 2000/02/03 09:00 [pubmed]
PHST- 2000/03/04 09:00 [medline]
PHST- 2000/02/03 09:00 [entrez]
AID - 10.1073/pnas.97.3.1056 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 2000 Feb 1;97(3):1056-61. doi: 10.1073/pnas.97.3.1056.