Subcellular localization and nucleosome specificity of yeast histone acetyltransferases
We have previously reported [López-Rodas et al. (1989) J. Biol. Chem. 264, 19028-19033] that the yeast Saccharomyces cerevisiae contains four histone acetyltransferases, which can be resolved by ion-exchange chromatography, and their specificity toward yeast free histones was studied. In the present...
Gespeichert in:
| Veröffentlicht in: | Biochemistry (Easton) 1991-04, Vol.30 (15), p.3728-3732 |
|---|---|
| Hauptverfasser: | , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 3732 |
|---|---|
| container_issue | 15 |
| container_start_page | 3728 |
| container_title | Biochemistry (Easton) |
| container_volume | 30 |
| creator | Lopez-Rodas, Gerardo Tordera, Vicente Mateo Sanchez del Pino, M Franco, Luis |
| description | We have previously reported [López-Rodas et al. (1989) J. Biol. Chem. 264, 19028-19033] that the yeast Saccharomyces cerevisiae contains four histone acetyltransferases, which can be resolved by ion-exchange chromatography, and their specificity toward yeast free histones was studied. In the present contribution we show that three of the enzymes are nuclear, type A histone acetyltransferases and they are able to acetylate nucleosome-bound histones. They differ in their histone specificity. Enzyme A1 acetylates H2A in chicken nucleosomes, although it is specific for yeast free H2B; histone acetyltransferase A2 is highly specific for H3, and histone acetyltransferase A3 preparations acetylate both H3 and H4 in nucleosomes. The fourth enzyme, which is located in the cytoplasm, does not accept nucleosomes as substrate, and it represents a canonical type B, H4-specific histone acetyltransferase. Finally, histone deacetylase activity is preferentially found in the nucleus. |
| doi_str_mv | 10.1021/bi00229a020 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_80508718</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>15923778</sourcerecordid><originalsourceid>FETCH-LOGICAL-a415t-4f5cfe6a16180e48fe017e4e77b659d7d83adee98b19e3017133f465902eed5a3</originalsourceid><addsrcrecordid>eNqFkM2L1DAYh4Mo67h68iz0oh6k-iZpmua4Dn7B-gG7snsLb9M3mLXTjEkLjn-9GWZYPQieQngefiQPY485vOQg-Ks-AAhhEATcYSuuBNSNMeouWwFAWwvTwn32IOebcm1ANyfsREDRRLdiVxdL72gclxFTNUaHY_iFc4hThdNQTYsbKea4oSpvyQUfXJh3VfTVjjDP1beQ5zhRhY7m3TgnnLKnhJnyQ3bP45jp0fE8ZV_fvrlcv6_PP7_7sD47r7Hhaq4br5ynFnnLO6Cm8wRcU0Na960ygx46iQOR6XpuSBbGpfRNQSCIBoXylD077G5T_LFQnu0m5P2HcKK4ZNuBgk7z7r8iV0ZIrffii4PoUsw5kbfbFDaYdpaD3fe2f_Uu9pPj7NJvaLh1j4ELf3rkmEtcXxK5kP9MGq1ASlO8-uCVovTzlmP6blsttbKXXy7sx6tr_elav7br4j8_-OiyvYlLmkrlf77wN7oIpHA</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>15923778</pqid></control><display><type>article</type><title>Subcellular localization and nucleosome specificity of yeast histone acetyltransferases</title><source>MEDLINE</source><source>ACS Publications</source><creator>Lopez-Rodas, Gerardo ; Tordera, Vicente ; Mateo Sanchez del Pino, M ; Franco, Luis</creator><creatorcontrib>Lopez-Rodas, Gerardo ; Tordera, Vicente ; Mateo Sanchez del Pino, M ; Franco, Luis</creatorcontrib><description>We have previously reported [López-Rodas et al. (1989) J. Biol. Chem. 264, 19028-19033] that the yeast Saccharomyces cerevisiae contains four histone acetyltransferases, which can be resolved by ion-exchange chromatography, and their specificity toward yeast free histones was studied. In the present contribution we show that three of the enzymes are nuclear, type A histone acetyltransferases and they are able to acetylate nucleosome-bound histones. They differ in their histone specificity. Enzyme A1 acetylates H2A in chicken nucleosomes, although it is specific for yeast free H2B; histone acetyltransferase A2 is highly specific for H3, and histone acetyltransferase A3 preparations acetylate both H3 and H4 in nucleosomes. The fourth enzyme, which is located in the cytoplasm, does not accept nucleosomes as substrate, and it represents a canonical type B, H4-specific histone acetyltransferase. Finally, histone deacetylase activity is preferentially found in the nucleus.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi00229a020</identifier><identifier>PMID: 2015228</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Acetyltransferases - metabolism ; Amidohydrolases - metabolism ; Analytical, structural and metabolic biochemistry ; Biological and medical sciences ; Cell Nucleus - enzymology ; Chromatography, Ion Exchange ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; Histone Acetyltransferases ; Histones - metabolism ; Nucleosomes - enzymology ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - enzymology ; Saccharomyces cerevisiae Proteins ; Substrate Specificity ; Transferases</subject><ispartof>Biochemistry (Easton), 1991-04, Vol.30 (15), p.3728-3732</ispartof><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a415t-4f5cfe6a16180e48fe017e4e77b659d7d83adee98b19e3017133f465902eed5a3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/bi00229a020$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi00229a020$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,780,784,2765,27076,27924,27925,56738,56788</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19750339$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2015228$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lopez-Rodas, Gerardo</creatorcontrib><creatorcontrib>Tordera, Vicente</creatorcontrib><creatorcontrib>Mateo Sanchez del Pino, M</creatorcontrib><creatorcontrib>Franco, Luis</creatorcontrib><title>Subcellular localization and nucleosome specificity of yeast histone acetyltransferases</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>We have previously reported [López-Rodas et al. (1989) J. Biol. Chem. 264, 19028-19033] that the yeast Saccharomyces cerevisiae contains four histone acetyltransferases, which can be resolved by ion-exchange chromatography, and their specificity toward yeast free histones was studied. In the present contribution we show that three of the enzymes are nuclear, type A histone acetyltransferases and they are able to acetylate nucleosome-bound histones. They differ in their histone specificity. Enzyme A1 acetylates H2A in chicken nucleosomes, although it is specific for yeast free H2B; histone acetyltransferase A2 is highly specific for H3, and histone acetyltransferase A3 preparations acetylate both H3 and H4 in nucleosomes. The fourth enzyme, which is located in the cytoplasm, does not accept nucleosomes as substrate, and it represents a canonical type B, H4-specific histone acetyltransferase. Finally, histone deacetylase activity is preferentially found in the nucleus.</description><subject>Acetyltransferases - metabolism</subject><subject>Amidohydrolases - metabolism</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>Cell Nucleus - enzymology</subject><subject>Chromatography, Ion Exchange</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Histone Acetyltransferases</subject><subject>Histones - metabolism</subject><subject>Nucleosomes - enzymology</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - enzymology</subject><subject>Saccharomyces cerevisiae Proteins</subject><subject>Substrate Specificity</subject><subject>Transferases</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkM2L1DAYh4Mo67h68iz0oh6k-iZpmua4Dn7B-gG7snsLb9M3mLXTjEkLjn-9GWZYPQieQngefiQPY485vOQg-Ks-AAhhEATcYSuuBNSNMeouWwFAWwvTwn32IOebcm1ANyfsREDRRLdiVxdL72gclxFTNUaHY_iFc4hThdNQTYsbKea4oSpvyQUfXJh3VfTVjjDP1beQ5zhRhY7m3TgnnLKnhJnyQ3bP45jp0fE8ZV_fvrlcv6_PP7_7sD47r7Hhaq4br5ynFnnLO6Cm8wRcU0Na960ygx46iQOR6XpuSBbGpfRNQSCIBoXylD077G5T_LFQnu0m5P2HcKK4ZNuBgk7z7r8iV0ZIrffii4PoUsw5kbfbFDaYdpaD3fe2f_Uu9pPj7NJvaLh1j4ELf3rkmEtcXxK5kP9MGq1ASlO8-uCVovTzlmP6blsttbKXXy7sx6tr_elav7br4j8_-OiyvYlLmkrlf77wN7oIpHA</recordid><startdate>19910416</startdate><enddate>19910416</enddate><creator>Lopez-Rodas, Gerardo</creator><creator>Tordera, Vicente</creator><creator>Mateo Sanchez del Pino, M</creator><creator>Franco, Luis</creator><general>American Chemical Society</general><scope>BSCLL</scope><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>M7N</scope><scope>7X8</scope></search><sort><creationdate>19910416</creationdate><title>Subcellular localization and nucleosome specificity of yeast histone acetyltransferases</title><author>Lopez-Rodas, Gerardo ; Tordera, Vicente ; Mateo Sanchez del Pino, M ; Franco, Luis</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a415t-4f5cfe6a16180e48fe017e4e77b659d7d83adee98b19e3017133f465902eed5a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Acetyltransferases - metabolism</topic><topic>Amidohydrolases - metabolism</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Biological and medical sciences</topic><topic>Cell Nucleus - enzymology</topic><topic>Chromatography, Ion Exchange</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Histone Acetyltransferases</topic><topic>Histones - metabolism</topic><topic>Nucleosomes - enzymology</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - enzymology</topic><topic>Saccharomyces cerevisiae Proteins</topic><topic>Substrate Specificity</topic><topic>Transferases</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lopez-Rodas, Gerardo</creatorcontrib><creatorcontrib>Tordera, Vicente</creatorcontrib><creatorcontrib>Mateo Sanchez del Pino, M</creatorcontrib><creatorcontrib>Franco, Luis</creatorcontrib><collection>Istex</collection><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>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lopez-Rodas, Gerardo</au><au>Tordera, Vicente</au><au>Mateo Sanchez del Pino, M</au><au>Franco, Luis</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Subcellular localization and nucleosome specificity of yeast histone acetyltransferases</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>1991-04-16</date><risdate>1991</risdate><volume>30</volume><issue>15</issue><spage>3728</spage><epage>3732</epage><pages>3728-3732</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>We have previously reported [López-Rodas et al. (1989) J. Biol. Chem. 264, 19028-19033] that the yeast Saccharomyces cerevisiae contains four histone acetyltransferases, which can be resolved by ion-exchange chromatography, and their specificity toward yeast free histones was studied. In the present contribution we show that three of the enzymes are nuclear, type A histone acetyltransferases and they are able to acetylate nucleosome-bound histones. They differ in their histone specificity. Enzyme A1 acetylates H2A in chicken nucleosomes, although it is specific for yeast free H2B; histone acetyltransferase A2 is highly specific for H3, and histone acetyltransferase A3 preparations acetylate both H3 and H4 in nucleosomes. The fourth enzyme, which is located in the cytoplasm, does not accept nucleosomes as substrate, and it represents a canonical type B, H4-specific histone acetyltransferase. Finally, histone deacetylase activity is preferentially found in the nucleus.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>2015228</pmid><doi>10.1021/bi00229a020</doi><tpages>5</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0006-2960 |
| ispartof | Biochemistry (Easton), 1991-04, Vol.30 (15), p.3728-3732 |
| issn | 0006-2960 1520-4995 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_80508718 |
| source | MEDLINE; ACS Publications |
| subjects | Acetyltransferases - metabolism Amidohydrolases - metabolism Analytical, structural and metabolic biochemistry Biological and medical sciences Cell Nucleus - enzymology Chromatography, Ion Exchange Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Histone Acetyltransferases Histones - metabolism Nucleosomes - enzymology Saccharomyces cerevisiae Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae Proteins Substrate Specificity Transferases |
| title | Subcellular localization and nucleosome specificity of yeast histone acetyltransferases |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-06T08%3A50%3A14IST&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=Subcellular%20localization%20and%20nucleosome%20specificity%20of%20yeast%20histone%20acetyltransferases&rft.jtitle=Biochemistry%20(Easton)&rft.au=Lopez-Rodas,%20Gerardo&rft.date=1991-04-16&rft.volume=30&rft.issue=15&rft.spage=3728&rft.epage=3732&rft.pages=3728-3732&rft.issn=0006-2960&rft.eissn=1520-4995&rft_id=info:doi/10.1021/bi00229a020&rft_dat=%3Cproquest_cross%3E15923778%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=15923778&rft_id=info:pmid/2015228&rfr_iscdi=true |