Site specificity of pea histone acetyltransferase B in vitro
Histone acetyltransferase B from pea embryonic axes has been purified approximately 300-fold by a combination of chromatographic procedures, including affinity chromatography on histone-agarose. The enzyme preparation has been used for the in vitro transfer of acetyl groups from [1-14C]acetyl-CoA to...
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| Veröffentlicht in: | The Journal of biological chemistry 1993-06, Vol.268 (18), p.13248-13252 |
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| container_title | The Journal of biological chemistry |
| container_volume | 268 |
| creator | Mingarro, I Sendra, R Salvador, M.L Franco, L |
| description | Histone acetyltransferase B from pea embryonic axes has been purified approximately 300-fold by a combination of chromatographic procedures, including affinity chromatography on histone-agarose. The enzyme preparation has been used for the in vitro transfer of acetyl groups from [1-14C]acetyl-CoA to non-acetylated pea histone H4. Up to three acetyl groups can be introduced into the histone. The resulting mono-, di-, and triacetylated H4 isoforms were separated and sequenced to determine the acetylated sites. Only sites 5, 12, and 16 were used by histone acetyltransferase B, but no clear preference among them was observed. The absence of modification of other potentially acetylatable sites is another indication that acetylation of the different lysine residues in the N-terminal H4 tail serves as a specific signal in different nuclear processes |
| doi_str_mv | 10.1016/S0021-9258(19)38644-2 |
| format | Article |
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The enzyme preparation has been used for the in vitro transfer of acetyl groups from [1-14C]acetyl-CoA to non-acetylated pea histone H4. Up to three acetyl groups can be introduced into the histone. The resulting mono-, di-, and triacetylated H4 isoforms were separated and sequenced to determine the acetylated sites. Only sites 5, 12, and 16 were used by histone acetyltransferase B, but no clear preference among them was observed. 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Psychology ; HISTONAS ; HISTONE ; Histone Acetyltransferases ; Histones - chemistry ; Histones - metabolism ; Isoenzymes - isolation & purification ; Isoenzymes - metabolism ; Molecular Sequence Data ; PISUM SATIVUM ; Plants, Medicinal ; PURIFICACION ; PURIFICATION ; Saccharomyces cerevisiae Proteins ; Substrate Specificity ; Transferases</subject><ispartof>The Journal of biological chemistry, 1993-06, Vol.268 (18), p.13248-13252</ispartof><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3742-6e255f224597fdffd433872302afc72ea0e610563f55bc660c11d0d90b52bf163</citedby><cites>FETCH-LOGICAL-c3742-6e255f224597fdffd433872302afc72ea0e610563f55bc660c11d0d90b52bf163</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4829782$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8514763$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mingarro, I</creatorcontrib><creatorcontrib>Sendra, R</creatorcontrib><creatorcontrib>Salvador, M.L</creatorcontrib><creatorcontrib>Franco, L</creatorcontrib><title>Site specificity of pea histone acetyltransferase B in vitro</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Histone acetyltransferase B from pea embryonic axes has been purified approximately 300-fold by a combination of chromatographic procedures, including affinity chromatography on histone-agarose. The enzyme preparation has been used for the in vitro transfer of acetyl groups from [1-14C]acetyl-CoA to non-acetylated pea histone H4. Up to three acetyl groups can be introduced into the histone. The resulting mono-, di-, and triacetylated H4 isoforms were separated and sequenced to determine the acetylated sites. Only sites 5, 12, and 16 were used by histone acetyltransferase B, but no clear preference among them was observed. The absence of modification of other potentially acetylatable sites is another indication that acetylation of the different lysine residues in the N-terminal H4 tail serves as a specific signal in different nuclear processes</description><subject>Acetylation</subject><subject>Acetyltransferases - isolation & purification</subject><subject>Acetyltransferases - metabolism</subject><subject>ACILTRANSFERASA</subject><subject>ACYLTRANSFERASE</subject><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>Chromatography, Affinity</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fabaceae - enzymology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>HISTONAS</subject><subject>HISTONE</subject><subject>Histone Acetyltransferases</subject><subject>Histones - chemistry</subject><subject>Histones - metabolism</subject><subject>Isoenzymes - isolation & purification</subject><subject>Isoenzymes - metabolism</subject><subject>Molecular Sequence Data</subject><subject>PISUM SATIVUM</subject><subject>Plants, Medicinal</subject><subject>PURIFICACION</subject><subject>PURIFICATION</subject><subject>Saccharomyces cerevisiae Proteins</subject><subject>Substrate Specificity</subject><subject>Transferases</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1rGzEQhkVoSdwkfyAQ2EMJzWEbafSxEuSShKYtBHpwArkJrXYUq6y9rrRO8L-vHBv32GFgDvPMvPAQcs7oV0aZuppSCqw2IPUXZi65VkLUcEAmjGpec8meP5DJHjkin3L-TUsJww7JoZZMNIpPyPU0jljlJfoYoo_juhpCtURXzWIehwVWzuO47sfkFjlgchmr2youqtc4puGEfAyuz3i6m8fk6f7b492P-uHX9593Nw-1542AWiFIGQCENE3oQugE57oBTsEF3wA6iopRqXiQsvVKUc9YRztDWwltYIofk4vt32Ua_qwwj3Yes8e-dwscVtk2sjFccf5fkClVMIACyi3o05BzwmCXKc5dWltG7UavfddrN-4sM_Zdr93cne8CVu0cu_3VzmfZf97tXfauD0Wbj3mPCQ2m0fAPm8WX2VtMaNs4-BnOLaiSV5qD0AU722LBDda9pPLpaWoEN0YL_he-pJSj</recordid><startdate>19930625</startdate><enddate>19930625</enddate><creator>Mingarro, I</creator><creator>Sendra, R</creator><creator>Salvador, M.L</creator><creator>Franco, L</creator><general>American Society for Biochemistry and Molecular Biology</general><scope>FBQ</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>7X8</scope></search><sort><creationdate>19930625</creationdate><title>Site specificity of pea histone acetyltransferase B in vitro</title><author>Mingarro, I ; Sendra, R ; Salvador, M.L ; Franco, L</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3742-6e255f224597fdffd433872302afc72ea0e610563f55bc660c11d0d90b52bf163</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Acetylation</topic><topic>Acetyltransferases - isolation & purification</topic><topic>Acetyltransferases - metabolism</topic><topic>ACILTRANSFERASA</topic><topic>ACYLTRANSFERASE</topic><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Biological and medical sciences</topic><topic>Chromatography, Affinity</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fabaceae - enzymology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>HISTONAS</topic><topic>HISTONE</topic><topic>Histone Acetyltransferases</topic><topic>Histones - chemistry</topic><topic>Histones - metabolism</topic><topic>Isoenzymes - isolation & purification</topic><topic>Isoenzymes - metabolism</topic><topic>Molecular Sequence Data</topic><topic>PISUM SATIVUM</topic><topic>Plants, Medicinal</topic><topic>PURIFICACION</topic><topic>PURIFICATION</topic><topic>Saccharomyces cerevisiae Proteins</topic><topic>Substrate Specificity</topic><topic>Transferases</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mingarro, I</creatorcontrib><creatorcontrib>Sendra, R</creatorcontrib><creatorcontrib>Salvador, M.L</creatorcontrib><creatorcontrib>Franco, L</creatorcontrib><collection>AGRIS</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>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mingarro, I</au><au>Sendra, R</au><au>Salvador, M.L</au><au>Franco, L</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Site specificity of pea histone acetyltransferase B in vitro</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1993-06-25</date><risdate>1993</risdate><volume>268</volume><issue>18</issue><spage>13248</spage><epage>13252</epage><pages>13248-13252</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>Histone acetyltransferase B from pea embryonic axes has been purified approximately 300-fold by a combination of chromatographic procedures, including affinity chromatography on histone-agarose. The enzyme preparation has been used for the in vitro transfer of acetyl groups from [1-14C]acetyl-CoA to non-acetylated pea histone H4. Up to three acetyl groups can be introduced into the histone. The resulting mono-, di-, and triacetylated H4 isoforms were separated and sequenced to determine the acetylated sites. Only sites 5, 12, and 16 were used by histone acetyltransferase B, but no clear preference among them was observed. The absence of modification of other potentially acetylatable sites is another indication that acetylation of the different lysine residues in the N-terminal H4 tail serves as a specific signal in different nuclear processes</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>8514763</pmid><doi>10.1016/S0021-9258(19)38644-2</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1993-06, Vol.268 (18), p.13248-13252 |
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| language | eng |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Acetylation Acetyltransferases - isolation & purification Acetyltransferases - metabolism ACILTRANSFERASA ACYLTRANSFERASE Amino Acid Sequence Analytical, structural and metabolic biochemistry Biological and medical sciences Chromatography, Affinity Electrophoresis, Polyacrylamide Gel Enzymes and enzyme inhibitors Fabaceae - enzymology Fundamental and applied biological sciences. Psychology HISTONAS HISTONE Histone Acetyltransferases Histones - chemistry Histones - metabolism Isoenzymes - isolation & purification Isoenzymes - metabolism Molecular Sequence Data PISUM SATIVUM Plants, Medicinal PURIFICACION PURIFICATION Saccharomyces cerevisiae Proteins Substrate Specificity Transferases |
| title | Site specificity of pea histone acetyltransferase B in vitro |
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