دورية أكاديمية
Characterization of a human RPD3 ortholog, HDAC3.
| العنوان: | Characterization of a human RPD3 ortholog, HDAC3. |
|---|---|
| المؤلفون: | Emiliani, Serena, Fischle, W, Van Lint, Carine, Al-Abed, Y, Verdin, Eric |
| المصدر: | Proceedings of the National Academy of Sciences of the United States of America, 95 (6 |
| سنة النشر: | 1998 |
| المجموعة: | DI-fusion : dépôt institutionnel de l'Université libre de Bruxelles (ULB) |
| مصطلحات موضوعية: | Sciences bio-médicales et agricoles, Amino Acid Sequence, Anti-Bacterial Agents -- pharmacology, Base Sequence, Butyric Acid, Butyric Acids -- pharmacology, DNA, Complementary -- genetics, Gene Expression, Gene Library, Histone Deacetylase 1, Histone Deacetylase Inhibitors, Histone Deacetylases -- genetics, Histone Deacetylases -- isolation & purification, Histone Deacetylases -- metabolism, Histones -- metabolism, Humans, Hydroxamic Acids -- pharmacology, Molecular Sequence Data, Nuclear Proteins -- genetics, Nuclear Proteins -- isolation & purification, Nucleosomes -- metabolism, Peptides, Sequence Homology, Amino Acid, Transcription Factors -- genetics |
| الوصف: | Histone acetylation levels in cells result from a dynamic equilibrium between competing histone acetylases and deacetylases. Changes in histone acetylation levels occur during both transcriptional activation and silencing. Cloning of the cDNA for a human histone deacetylase (HDAC1) has shown that it represents a human ortholog of the yeast transcriptional regulator RPD3. We have screened the expressed sequence tag database (National Center for Biotechnology Information) with the yeast RPD3 sequence and identified a human ortholog of RPD3, HDAC3. This cDNA encodes a protein of 428 amino acids with 58% sequence identity with HDAC1p. By using a specific polyclonal antiserum recognizing the C-terminal domain of HDAC3p and Western blotting, we detected a single approximately 49-kDa band in several tumor cell lines. HDAC3p is expressed predominantly in the nuclear compartment. Immunoprecipitation experiments with either an antiserum against HDAC3p or an anti-FLAG antiserum and a flagged HDAC3 cDNA showed that HDAc3p exhibits deacetylase activity both on free histones and on purified nucleosomes. This deacetylase activity is inhibited by trichostatin, trapoxin, and butyrate in vitro to the same degree as the deacetylase activity associated to HDAC1p. These observations identify another member of a growing family of human HDAC genes. ; Comparative Study ; Journal Article ; Research Support, U.S. Gov't, P.H.S. ; info:eu-repo/semantics/published |
| نوع الوثيقة: | article in journal/newspaper |
| وصف الملف: | 1 full-text file(s): application/pdf |
| اللغة: | English |
| العلاقة: | uri/info:pmid/9501169; uri/info:pmcid/PMC19648; https://dipot.ulb.ac.be/dspace/bitstream/2013/58212/4/PMC19648.pdfTest; http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/58212Test |
| الإتاحة: | http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/58212Test https://dipot.ulb.ac.be/dspace/bitstream/2013/58212/4/PMC19648.pdfTest |
| رقم الانضمام: | edsbas.3B67D94A |
| قاعدة البيانات: | BASE |
| الوصف غير متاح. |