Human ING1 Proteins Differentially Regulate Histone Acetylation
ING1 proteins are nuclear, growth inhibitory, and regulate apoptosis in different experimental systems. Here we show that similar to their yeast homologs, human ING1 proteins interact with proteins associated with histone acetyltransferase (HAT) activity, such as TRRAP, PCAF, CBP, and p300. Human IN...
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| Veröffentlicht in: | The Journal of biological chemistry 2002-08, Vol.277 (33), p.29832-29839 |
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| creator | Vieyra, Diego Loewith, Robbie Scott, Michelle Bonnefin, Paul Boisvert, Francois-Michel Cheema, Parneet Pastyryeva, Svitlana Meijer, Maria Johnston, Randal N. Bazett-Jones, David P. McMahon, Steven Cole, Michael D. Young, Dallan Riabowol, Karl |
| description | ING1 proteins are nuclear, growth inhibitory, and regulate apoptosis in different experimental systems. Here we show that similar to their yeast homologs, human ING1 proteins interact with proteins associated with histone acetyltransferase (HAT) activity, such as TRRAP, PCAF, CBP, and p300. Human ING1 immunocomplexes contain HAT activity, and overexpression of p33ING1b, but not of p47ING1a, induces hyperacetylation of histones H3 and H4, in vitro and in vivo at the single cell level. p47ING1a inhibits histone acetylation in vitro and in vivo and binds the histone deacetylase HDAC1. Finally, we present evidence indicating that p33ING1b affects the degree of physical association between proliferating cell nuclear antigen (PCNA) and p300, an association that has been proposed to link DNA repair to chromatin remodeling. Together with the finding that human ING1 proteins bind PCNA in a DNA damage-dependent manner, these data suggest that ING1 proteins provide a direct linkage between DNA repair, apoptosis, and chromatin remodeling via multiple HAT·ING1·PCNA protein complexes. |
| doi_str_mv | 10.1074/jbc.M200197200 |
| format | Article |
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Here we show that similar to their yeast homologs, human ING1 proteins interact with proteins associated with histone acetyltransferase (HAT) activity, such as TRRAP, PCAF, CBP, and p300. Human ING1 immunocomplexes contain HAT activity, and overexpression of p33ING1b, but not of p47ING1a, induces hyperacetylation of histones H3 and H4, in vitro and in vivo at the single cell level. p47ING1a inhibits histone acetylation in vitro and in vivo and binds the histone deacetylase HDAC1. Finally, we present evidence indicating that p33ING1b affects the degree of physical association between proliferating cell nuclear antigen (PCNA) and p300, an association that has been proposed to link DNA repair to chromatin remodeling. Together with the finding that human ING1 proteins bind PCNA in a DNA damage-dependent manner, these data suggest that ING1 proteins provide a direct linkage between DNA repair, apoptosis, and chromatin remodeling via multiple HAT·ING1·PCNA protein complexes.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M200197200</identifier><identifier>PMID: 12015309</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Acetylation ; Acetyltransferases - metabolism ; Apoptosis - physiology ; Cell Cycle Proteins ; Cell Line ; DNA-Binding Proteins ; Down-Regulation ; Genes, Tumor Suppressor ; Histone Acetyltransferases ; Histones - metabolism ; Humans ; Inhibitor of Growth Protein 1 ; Intracellular Signaling Peptides and Proteins ; Nuclear Proteins ; Proteins - metabolism ; Proteins - physiology ; Saccharomyces cerevisiae Proteins ; Tumor Suppressor Proteins</subject><ispartof>The Journal of biological chemistry, 2002-08, Vol.277 (33), p.29832-29839</ispartof><rights>2002 © 2002 ASBMB. 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Here we show that similar to their yeast homologs, human ING1 proteins interact with proteins associated with histone acetyltransferase (HAT) activity, such as TRRAP, PCAF, CBP, and p300. Human ING1 immunocomplexes contain HAT activity, and overexpression of p33ING1b, but not of p47ING1a, induces hyperacetylation of histones H3 and H4, in vitro and in vivo at the single cell level. p47ING1a inhibits histone acetylation in vitro and in vivo and binds the histone deacetylase HDAC1. Finally, we present evidence indicating that p33ING1b affects the degree of physical association between proliferating cell nuclear antigen (PCNA) and p300, an association that has been proposed to link DNA repair to chromatin remodeling. Together with the finding that human ING1 proteins bind PCNA in a DNA damage-dependent manner, these data suggest that ING1 proteins provide a direct linkage between DNA repair, apoptosis, and chromatin remodeling via multiple HAT·ING1·PCNA protein complexes.</description><subject>Acetylation</subject><subject>Acetyltransferases - metabolism</subject><subject>Apoptosis - physiology</subject><subject>Cell Cycle Proteins</subject><subject>Cell Line</subject><subject>DNA-Binding Proteins</subject><subject>Down-Regulation</subject><subject>Genes, Tumor Suppressor</subject><subject>Histone Acetyltransferases</subject><subject>Histones - metabolism</subject><subject>Humans</subject><subject>Inhibitor of Growth Protein 1</subject><subject>Intracellular Signaling Peptides and Proteins</subject><subject>Nuclear Proteins</subject><subject>Proteins - metabolism</subject><subject>Proteins - physiology</subject><subject>Saccharomyces cerevisiae Proteins</subject><subject>Tumor Suppressor Proteins</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkMtLxDAQh4Mouj6uHqUH8dZ1krRNehLxtYIvRMFbaJOJG-lDk1bZ_97ILngS5zADw_cbho-QfQpTCiI7fqv19JYB0FLEvkYmFCRPeU5f1skEgNG0ZLncItshvEGsrKSbZIsyoDmHckJOZmNbdcn13RVNHnw_oOtCcu6sRY_d4KqmWSSP-Do21YDJzIWh7zA51Tgs4sb13S7ZsFUTcG81d8jz5cXT2Sy9ub-6Pju9SXUOckgNZJJpw0pkteCi5pmmkBW25sALmTODeVZbaRjDorSmEkLLWlTWCGkt5MB3yNHy7rvvP0YMg2pd0Ng0VYf9GJSgpSx4zv8FqcwKSSWN4HQJat-H4NGqd-_ayi8UBfXjVkW36tdtDBysLo91i-YXX8mMwOESmLvX-ZfzqGrX6zm2igmhOFeslJxFTC4xjL4-HXoVtMNOo4kRPSjTu79e-AZ9XpJR</recordid><startdate>20020816</startdate><enddate>20020816</enddate><creator>Vieyra, Diego</creator><creator>Loewith, Robbie</creator><creator>Scott, Michelle</creator><creator>Bonnefin, Paul</creator><creator>Boisvert, Francois-Michel</creator><creator>Cheema, Parneet</creator><creator>Pastyryeva, Svitlana</creator><creator>Meijer, Maria</creator><creator>Johnston, Randal N.</creator><creator>Bazett-Jones, David P.</creator><creator>McMahon, Steven</creator><creator>Cole, Michael D.</creator><creator>Young, Dallan</creator><creator>Riabowol, Karl</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</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>20020816</creationdate><title>Human ING1 Proteins Differentially Regulate Histone Acetylation</title><author>Vieyra, Diego ; Loewith, Robbie ; Scott, Michelle ; Bonnefin, Paul ; Boisvert, Francois-Michel ; Cheema, Parneet ; Pastyryeva, Svitlana ; Meijer, Maria ; Johnston, Randal N. ; Bazett-Jones, David P. ; McMahon, Steven ; Cole, Michael D. ; Young, Dallan ; Riabowol, Karl</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c508t-d0482cd29e2b737b34c1046fb3036852de54bf8d22e69fda77c8b7afd78ff0503</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Acetylation</topic><topic>Acetyltransferases - metabolism</topic><topic>Apoptosis - physiology</topic><topic>Cell Cycle Proteins</topic><topic>Cell Line</topic><topic>DNA-Binding Proteins</topic><topic>Down-Regulation</topic><topic>Genes, Tumor Suppressor</topic><topic>Histone Acetyltransferases</topic><topic>Histones - metabolism</topic><topic>Humans</topic><topic>Inhibitor of Growth Protein 1</topic><topic>Intracellular Signaling Peptides and Proteins</topic><topic>Nuclear Proteins</topic><topic>Proteins - metabolism</topic><topic>Proteins - physiology</topic><topic>Saccharomyces cerevisiae Proteins</topic><topic>Tumor Suppressor Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Vieyra, Diego</creatorcontrib><creatorcontrib>Loewith, Robbie</creatorcontrib><creatorcontrib>Scott, Michelle</creatorcontrib><creatorcontrib>Bonnefin, Paul</creatorcontrib><creatorcontrib>Boisvert, Francois-Michel</creatorcontrib><creatorcontrib>Cheema, Parneet</creatorcontrib><creatorcontrib>Pastyryeva, Svitlana</creatorcontrib><creatorcontrib>Meijer, Maria</creatorcontrib><creatorcontrib>Johnston, Randal N.</creatorcontrib><creatorcontrib>Bazett-Jones, David P.</creatorcontrib><creatorcontrib>McMahon, Steven</creatorcontrib><creatorcontrib>Cole, Michael D.</creatorcontrib><creatorcontrib>Young, Dallan</creatorcontrib><creatorcontrib>Riabowol, Karl</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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>Vieyra, Diego</au><au>Loewith, Robbie</au><au>Scott, Michelle</au><au>Bonnefin, Paul</au><au>Boisvert, Francois-Michel</au><au>Cheema, Parneet</au><au>Pastyryeva, Svitlana</au><au>Meijer, Maria</au><au>Johnston, Randal N.</au><au>Bazett-Jones, David P.</au><au>McMahon, Steven</au><au>Cole, Michael D.</au><au>Young, Dallan</au><au>Riabowol, Karl</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Human ING1 Proteins Differentially Regulate Histone Acetylation</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2002-08-16</date><risdate>2002</risdate><volume>277</volume><issue>33</issue><spage>29832</spage><epage>29839</epage><pages>29832-29839</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>ING1 proteins are nuclear, growth inhibitory, and regulate apoptosis in different experimental systems. 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| subjects | Acetylation Acetyltransferases - metabolism Apoptosis - physiology Cell Cycle Proteins Cell Line DNA-Binding Proteins Down-Regulation Genes, Tumor Suppressor Histone Acetyltransferases Histones - metabolism Humans Inhibitor of Growth Protein 1 Intracellular Signaling Peptides and Proteins Nuclear Proteins Proteins - metabolism Proteins - physiology Saccharomyces cerevisiae Proteins Tumor Suppressor Proteins |
| title | Human ING1 Proteins Differentially Regulate Histone Acetylation |
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