TY - JOUR
T1 - SAP30, a novel protein conserved between human and yeast, is a component of a histone deacetylase complex
AU - Zhang, Yi
AU - Sun, Zu Wen
AU - Iratni, Rabah
AU - Erdjument-Bromage, Hediye
AU - Tempst, Paul
AU - Hampsey, Michael
AU - Reinberg, Danny
N1 - Funding Information:
We are grateful to Drs. C. A. Hassig and S. Schreiber for baculoviruses expressing HDAC1-Flag; to Drs. A. Verreault and B. Stillman for baculoviruses expressing RbAp48, for antibodies against RbAp46 and RbAp48, and for plasmids expressing GST-RbAps; to Drs. W.-M. Yang and E. Seto for anti-HDAC2 antibodies; to Dr. D. Allis for histone H3 and H4 antibodies; to Dr. D. Ayer for plasmids used in transfection assays; to Dr. D. Gottschling for telomeric-tagged yeast strains; Dr. D. Stillman for rpd3 and sin3 constructs; to Dr. S. Johnson for LexAop plasmids; to Drs. H.-J. Schueller and R. Gaber for INO1-lacZ and TRK2-lacZ reporter plasmids, respectively; to Dr. S.-J. Kim for yeast extracts and antibodies against Sin4; to Drs. X. Sun and S. Akoulitchev for assistance in partial purification of HeLa nuclear extracts; to Drs. G. Orphanides and T.-K. Kim for nonacetylated core histones and nucleosomes; and to K. Cabane for help in generating antibodies. We thank M. Lui and L. Lacomis for expert assistance with protein structural analysis, and S. Kao for preparing the nuclear extracts. We thank members of the Reinberg and Hampsey laboratories for stimulating discussions during the course of this work. We also thank Drs. C. Laherty and R. Eisenman for communicating results prior to publication. D. R. was supported by grants from the National Institutes of Health (GM-48518) and from the Howard Hughes Medical Institute. M. H. was supported by a grant from the National Institutes of Health (GM-39484). P. T. was supported by a grant from the National Science Foundation (DBI-9420123) and by a grant from the National Cancer Institute (5P309CA08748) to the Sloan-Kettering Structural Chemistry Laboratory.
PY - 1998/6
Y1 - 1998/6
N2 - Histone acetylation plays a key role in the regulation of eukaryotic gene expression. Recently, histone acetylation and deacetylation were found to be catalyzed by structurally distinct, multisubunit complexes that mediate, respectively, activation and repression of transcription. Here, we identify SAP30 as a novel component of the human histone deacetylase complex that includes Sin3, the histone deacetylases HDAC1 and HDAC2, histone binding proteins RbAp46 and RbAp48, as well as other polypeptides. Moreover, we describe a SAP30 homolog in yeast that is functionally related to Sin3 and the histone deacetylase Rpd3. The human SAP30 complex is active in deacetylating core histone octamers, but inactive in deacetylating nucleosomal histones due to the inability of the histone binding proteins RbAp46 and RbAp48 to gain access to nucleosomal histones. These results define SAP30 as a component of a histone deacetylase complex conserved among eukaryotic organisms.
AB - Histone acetylation plays a key role in the regulation of eukaryotic gene expression. Recently, histone acetylation and deacetylation were found to be catalyzed by structurally distinct, multisubunit complexes that mediate, respectively, activation and repression of transcription. Here, we identify SAP30 as a novel component of the human histone deacetylase complex that includes Sin3, the histone deacetylases HDAC1 and HDAC2, histone binding proteins RbAp46 and RbAp48, as well as other polypeptides. Moreover, we describe a SAP30 homolog in yeast that is functionally related to Sin3 and the histone deacetylase Rpd3. The human SAP30 complex is active in deacetylating core histone octamers, but inactive in deacetylating nucleosomal histones due to the inability of the histone binding proteins RbAp46 and RbAp48 to gain access to nucleosomal histones. These results define SAP30 as a component of a histone deacetylase complex conserved among eukaryotic organisms.
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U2 - 10.1016/S1097-2765(00)80102-1
DO - 10.1016/S1097-2765(00)80102-1
M3 - Article
C2 - 9651585
AN - SCOPUS:0032088533
SN - 1097-2765
VL - 1
SP - 1021
EP - 1031
JO - Molecular Cell
JF - Molecular Cell
IS - 7
ER -