The BRCA2 is a histone acetyltransferase
Patients carrying mutations in BRCA1 or BRCA2 tumor suppressor genes have shown to have high risk in developing breast and ovarian cancers. Two potential functions of BRCA2 were proposed which includes role in the regulation of transcription and also in DNA repair. Forty-five-amino acid region encod...
Gespeichert in:
Veröffentlicht in: | Oncogene 1998-04, Vol.16 (17), p.2283-2285 |
---|---|
Hauptverfasser: | , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 2285 |
---|---|
container_issue | 17 |
container_start_page | 2283 |
container_title | Oncogene |
container_volume | 16 |
creator | SIDDIQUE, H ZOU, J.-P RAO, V. N REDDY, E. S. P |
description | Patients carrying mutations in BRCA1 or BRCA2 tumor suppressor genes have shown to have high risk in developing breast and ovarian cancers. Two potential functions of BRCA2 were proposed which includes role in the regulation of transcription and also in DNA repair. Forty-five-amino acid region encoded by exon 3 of BRCA2 was shown to have transcriptional activation function. Recent studies of the several enzymes involved in acetylation and deacetylation of histone residues have revealed a possible relationship between gene transcriptional activation and histone acetylation. Since BRCA2 appear to function as a transcriptional factor, we have tested for Histone acetyl transferase (HAT) activity of BRCA2. Here, we present evidence that BRCA2 has intrinsic HAT activity, which maps to the amino-terminal region of BRCA2. Our results demonstrate that BRCA2 proteins acetylate primarily H3 and H4 of free histones. These observations suggest that HAT activity of BRCA2 may play an important role in the regulation of transcription and tumor suppressor function. |
doi_str_mv | 10.1038/sj.onc.1202003 |
format | Article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_79918262</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>16427676</sourcerecordid><originalsourceid>FETCH-LOGICAL-c418t-b879386323d5c13e8a01ad3eb50f6dfbdf6b53b3976e00403f7a496c5c933a83</originalsourceid><addsrcrecordid>eNqFkM9LwzAYhoMoc06v3oSCIl5av-RrkuY4h79gIMjuIU1T1tK1M-kO--_tWNnBi6fv8D7vC99DyC2FhAJmz6FOutYmlAEDwDMypakUMecqPSdTUBxixZBdkqsQagCQCtiETJSgKkM5JU-rtYtevhdzFlUhMtG6Cn3XushY1--b3ps2lM6b4K7JRWma4G7GOyOrt9fV4iNefr1_LubL2KY06-M8kwozgQwLbim6zAA1BbqcQymKMi9KkXPMUUnhAFLAUppUCcutQjQZzsjjcXbru5-dC73eVMG6pjGt63ZBS6VoxgT7F6QiZVJIMYD3f8C62_l2-EEzkVImU84OVHKkrO9C8K7UW19tjN9rCvogWodaD6L1KHoo3I2zu3zjihM-mh3yhzE3wZqmHEzaKpwwxlAIyfEX5_SDNA</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2641274526</pqid></control><display><type>article</type><title>The BRCA2 is a histone acetyltransferase</title><source>MEDLINE</source><source>Nature Journals Online</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>Alma/SFX Local Collection</source><creator>SIDDIQUE, H ; ZOU, J.-P ; RAO, V. N ; REDDY, E. S. P</creator><creatorcontrib>SIDDIQUE, H ; ZOU, J.-P ; RAO, V. N ; REDDY, E. S. P</creatorcontrib><description>Patients carrying mutations in BRCA1 or BRCA2 tumor suppressor genes have shown to have high risk in developing breast and ovarian cancers. Two potential functions of BRCA2 were proposed which includes role in the regulation of transcription and also in DNA repair. Forty-five-amino acid region encoded by exon 3 of BRCA2 was shown to have transcriptional activation function. Recent studies of the several enzymes involved in acetylation and deacetylation of histone residues have revealed a possible relationship between gene transcriptional activation and histone acetylation. Since BRCA2 appear to function as a transcriptional factor, we have tested for Histone acetyl transferase (HAT) activity of BRCA2. Here, we present evidence that BRCA2 has intrinsic HAT activity, which maps to the amino-terminal region of BRCA2. Our results demonstrate that BRCA2 proteins acetylate primarily H3 and H4 of free histones. These observations suggest that HAT activity of BRCA2 may play an important role in the regulation of transcription and tumor suppressor function.</description><identifier>ISSN: 0950-9232</identifier><identifier>EISSN: 1476-5594</identifier><identifier>DOI: 10.1038/sj.onc.1202003</identifier><identifier>PMID: 9619837</identifier><language>eng</language><publisher>Basingstoke: Nature Publishing</publisher><subject>Acetylation ; Acetyltransferases - genetics ; Acetyltransferases - physiology ; Biological and medical sciences ; BRCA1 protein ; BRCA2 Protein ; Breast ; Breast Neoplasms - enzymology ; Breast Neoplasms - genetics ; Cell physiology ; Cell transformation and carcinogenesis. Action of oncogenes and antioncogenes ; Deacetylation ; DNA repair ; Female ; Fundamental and applied biological sciences. Psychology ; Gene mapping ; Gene regulation ; Genetic Markers ; Histone acetyltransferase ; Histone Acetyltransferases ; Histones - metabolism ; Humans ; Molecular and cellular biology ; Neoplasm Proteins - genetics ; Neoplasm Proteins - physiology ; Ovarian cancer ; Ovarian Neoplasms - enzymology ; Ovarian Neoplasms - genetics ; Saccharomyces cerevisiae Proteins ; Transcription activation ; Transcription Factors - genetics ; Transcription Factors - physiology ; Tumor suppressor genes ; Tumors ; Yeast</subject><ispartof>Oncogene, 1998-04, Vol.16 (17), p.2283-2285</ispartof><rights>1998 INIST-CNRS</rights><rights>Macmillan Publishers Limited 1998.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c418t-b879386323d5c13e8a01ad3eb50f6dfbdf6b53b3976e00403f7a496c5c933a83</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,782,786,27933,27934</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=2236675$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9619837$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>SIDDIQUE, H</creatorcontrib><creatorcontrib>ZOU, J.-P</creatorcontrib><creatorcontrib>RAO, V. N</creatorcontrib><creatorcontrib>REDDY, E. S. P</creatorcontrib><title>The BRCA2 is a histone acetyltransferase</title><title>Oncogene</title><addtitle>Oncogene</addtitle><description>Patients carrying mutations in BRCA1 or BRCA2 tumor suppressor genes have shown to have high risk in developing breast and ovarian cancers. Two potential functions of BRCA2 were proposed which includes role in the regulation of transcription and also in DNA repair. Forty-five-amino acid region encoded by exon 3 of BRCA2 was shown to have transcriptional activation function. Recent studies of the several enzymes involved in acetylation and deacetylation of histone residues have revealed a possible relationship between gene transcriptional activation and histone acetylation. Since BRCA2 appear to function as a transcriptional factor, we have tested for Histone acetyl transferase (HAT) activity of BRCA2. Here, we present evidence that BRCA2 has intrinsic HAT activity, which maps to the amino-terminal region of BRCA2. Our results demonstrate that BRCA2 proteins acetylate primarily H3 and H4 of free histones. These observations suggest that HAT activity of BRCA2 may play an important role in the regulation of transcription and tumor suppressor function.</description><subject>Acetylation</subject><subject>Acetyltransferases - genetics</subject><subject>Acetyltransferases - physiology</subject><subject>Biological and medical sciences</subject><subject>BRCA1 protein</subject><subject>BRCA2 Protein</subject><subject>Breast</subject><subject>Breast Neoplasms - enzymology</subject><subject>Breast Neoplasms - genetics</subject><subject>Cell physiology</subject><subject>Cell transformation and carcinogenesis. Action of oncogenes and antioncogenes</subject><subject>Deacetylation</subject><subject>DNA repair</subject><subject>Female</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene mapping</subject><subject>Gene regulation</subject><subject>Genetic Markers</subject><subject>Histone acetyltransferase</subject><subject>Histone Acetyltransferases</subject><subject>Histones - metabolism</subject><subject>Humans</subject><subject>Molecular and cellular biology</subject><subject>Neoplasm Proteins - genetics</subject><subject>Neoplasm Proteins - physiology</subject><subject>Ovarian cancer</subject><subject>Ovarian Neoplasms - enzymology</subject><subject>Ovarian Neoplasms - genetics</subject><subject>Saccharomyces cerevisiae Proteins</subject><subject>Transcription activation</subject><subject>Transcription Factors - genetics</subject><subject>Transcription Factors - physiology</subject><subject>Tumor suppressor genes</subject><subject>Tumors</subject><subject>Yeast</subject><issn>0950-9232</issn><issn>1476-5594</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkM9LwzAYhoMoc06v3oSCIl5av-RrkuY4h79gIMjuIU1T1tK1M-kO--_tWNnBi6fv8D7vC99DyC2FhAJmz6FOutYmlAEDwDMypakUMecqPSdTUBxixZBdkqsQagCQCtiETJSgKkM5JU-rtYtevhdzFlUhMtG6Cn3XushY1--b3ps2lM6b4K7JRWma4G7GOyOrt9fV4iNefr1_LubL2KY06-M8kwozgQwLbim6zAA1BbqcQymKMi9KkXPMUUnhAFLAUppUCcutQjQZzsjjcXbru5-dC73eVMG6pjGt63ZBS6VoxgT7F6QiZVJIMYD3f8C62_l2-EEzkVImU84OVHKkrO9C8K7UW19tjN9rCvogWodaD6L1KHoo3I2zu3zjihM-mh3yhzE3wZqmHEzaKpwwxlAIyfEX5_SDNA</recordid><startdate>19980430</startdate><enddate>19980430</enddate><creator>SIDDIQUE, H</creator><creator>ZOU, J.-P</creator><creator>RAO, V. N</creator><creator>REDDY, E. S. P</creator><general>Nature Publishing</general><general>Nature Publishing Group</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19980430</creationdate><title>The BRCA2 is a histone acetyltransferase</title><author>SIDDIQUE, H ; ZOU, J.-P ; RAO, V. N ; REDDY, E. S. P</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c418t-b879386323d5c13e8a01ad3eb50f6dfbdf6b53b3976e00403f7a496c5c933a83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Acetylation</topic><topic>Acetyltransferases - genetics</topic><topic>Acetyltransferases - physiology</topic><topic>Biological and medical sciences</topic><topic>BRCA1 protein</topic><topic>BRCA2 Protein</topic><topic>Breast</topic><topic>Breast Neoplasms - enzymology</topic><topic>Breast Neoplasms - genetics</topic><topic>Cell physiology</topic><topic>Cell transformation and carcinogenesis. Action of oncogenes and antioncogenes</topic><topic>Deacetylation</topic><topic>DNA repair</topic><topic>Female</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene mapping</topic><topic>Gene regulation</topic><topic>Genetic Markers</topic><topic>Histone acetyltransferase</topic><topic>Histone Acetyltransferases</topic><topic>Histones - metabolism</topic><topic>Humans</topic><topic>Molecular and cellular biology</topic><topic>Neoplasm Proteins - genetics</topic><topic>Neoplasm Proteins - physiology</topic><topic>Ovarian cancer</topic><topic>Ovarian Neoplasms - enzymology</topic><topic>Ovarian Neoplasms - genetics</topic><topic>Saccharomyces cerevisiae Proteins</topic><topic>Transcription activation</topic><topic>Transcription Factors - genetics</topic><topic>Transcription Factors - physiology</topic><topic>Tumor suppressor genes</topic><topic>Tumors</topic><topic>Yeast</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>SIDDIQUE, H</creatorcontrib><creatorcontrib>ZOU, J.-P</creatorcontrib><creatorcontrib>RAO, V. N</creatorcontrib><creatorcontrib>REDDY, E. S. P</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Oncogene</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>SIDDIQUE, H</au><au>ZOU, J.-P</au><au>RAO, V. N</au><au>REDDY, E. S. P</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The BRCA2 is a histone acetyltransferase</atitle><jtitle>Oncogene</jtitle><addtitle>Oncogene</addtitle><date>1998-04-30</date><risdate>1998</risdate><volume>16</volume><issue>17</issue><spage>2283</spage><epage>2285</epage><pages>2283-2285</pages><issn>0950-9232</issn><eissn>1476-5594</eissn><abstract>Patients carrying mutations in BRCA1 or BRCA2 tumor suppressor genes have shown to have high risk in developing breast and ovarian cancers. Two potential functions of BRCA2 were proposed which includes role in the regulation of transcription and also in DNA repair. Forty-five-amino acid region encoded by exon 3 of BRCA2 was shown to have transcriptional activation function. Recent studies of the several enzymes involved in acetylation and deacetylation of histone residues have revealed a possible relationship between gene transcriptional activation and histone acetylation. Since BRCA2 appear to function as a transcriptional factor, we have tested for Histone acetyl transferase (HAT) activity of BRCA2. Here, we present evidence that BRCA2 has intrinsic HAT activity, which maps to the amino-terminal region of BRCA2. Our results demonstrate that BRCA2 proteins acetylate primarily H3 and H4 of free histones. These observations suggest that HAT activity of BRCA2 may play an important role in the regulation of transcription and tumor suppressor function.</abstract><cop>Basingstoke</cop><pub>Nature Publishing</pub><pmid>9619837</pmid><doi>10.1038/sj.onc.1202003</doi><tpages>3</tpages><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0950-9232 |
ispartof | Oncogene, 1998-04, Vol.16 (17), p.2283-2285 |
issn | 0950-9232 1476-5594 |
language | eng |
recordid | cdi_proquest_miscellaneous_79918262 |
source | MEDLINE; Nature Journals Online; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
subjects | Acetylation Acetyltransferases - genetics Acetyltransferases - physiology Biological and medical sciences BRCA1 protein BRCA2 Protein Breast Breast Neoplasms - enzymology Breast Neoplasms - genetics Cell physiology Cell transformation and carcinogenesis. Action of oncogenes and antioncogenes Deacetylation DNA repair Female Fundamental and applied biological sciences. Psychology Gene mapping Gene regulation Genetic Markers Histone acetyltransferase Histone Acetyltransferases Histones - metabolism Humans Molecular and cellular biology Neoplasm Proteins - genetics Neoplasm Proteins - physiology Ovarian cancer Ovarian Neoplasms - enzymology Ovarian Neoplasms - genetics Saccharomyces cerevisiae Proteins Transcription activation Transcription Factors - genetics Transcription Factors - physiology Tumor suppressor genes Tumors Yeast |
title | The BRCA2 is a histone acetyltransferase |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-11-30T04%3A26%3A55IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=The%20BRCA2%20is%20a%20histone%20acetyltransferase&rft.jtitle=Oncogene&rft.au=SIDDIQUE,%20H&rft.date=1998-04-30&rft.volume=16&rft.issue=17&rft.spage=2283&rft.epage=2285&rft.pages=2283-2285&rft.issn=0950-9232&rft.eissn=1476-5594&rft_id=info:doi/10.1038/sj.onc.1202003&rft_dat=%3Cproquest_cross%3E16427676%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2641274526&rft_id=info:pmid/9619837&rfr_iscdi=true |