Polyamines inhibit the yeast histone deacetylase
n-Butyrate inhibits the histone deacetylase from higher cells, but has little effect on the enzyme activity in Saccharomyces cerevisiae. Spermine and spermidine were therefore tested as potential yeast deacetylase inhibitors and found to inhibit fully the enzyme at 2 and 5 mM, respectively. The util...
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Veröffentlicht in: | FEBS letters 1987-08, Vol.220 (1), p.79-83 |
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creator | Vu, Quang A. Zhang, Dong-er Chroneos, Zissis C. Nelson, Daniel A. |
description | n-Butyrate inhibits the histone deacetylase from higher cells, but has little effect on the enzyme activity in
Saccharomyces cerevisiae. Spermine and spermidine were therefore tested as potential yeast deacetylase inhibitors and found to inhibit fully the enzyme at 2 and 5 mM, respectively. The utility of these inhibitors was demonstrated by showing that 2 mM spermine substantially increased the incorporation of [
3H]acetate into histone in a yeast nuclear acetyltransferase assay. |
doi_str_mv | 10.1016/0014-5793(87)80879-7 |
format | Article |
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Saccharomyces cerevisiae. Spermine and spermidine were therefore tested as potential yeast deacetylase inhibitors and found to inhibit fully the enzyme at 2 and 5 mM, respectively. The utility of these inhibitors was demonstrated by showing that 2 mM spermine substantially increased the incorporation of [
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Saccharomyces cerevisiae. Spermine and spermidine were therefore tested as potential yeast deacetylase inhibitors and found to inhibit fully the enzyme at 2 and 5 mM, respectively. The utility of these inhibitors was demonstrated by showing that 2 mM spermine substantially increased the incorporation of [
3H]acetate into histone in a yeast nuclear acetyltransferase assay.</description><subject>Acetates - metabolism</subject><subject>Amidohydrolases - antagonists & inhibitors</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Histone deacetylase</subject><subject>Histone Deacetylase Inhibitors</subject><subject>Hydrolases</subject><subject>Mes, 4-morpholineethanesulfonic acid</subject><subject>n-Butyrate</subject><subject>PMSF, phenylmethylsulfonyl fluoride</subject><subject>Polyamines - pharmacology</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - enzymology</subject><subject>Spermidine</subject><subject>Spermidine - pharmacology</subject><subject>Spermine</subject><subject>Spermine - pharmacology</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkEFLwzAUx4Moc06_gUIPInqo5jVpk10EHZsKAz3oOaTpC4t07Ww6pd_edBs7iqeQ9_-995IfIedAb4FCdkcp8DgVY3YtxY2kUoxjcUCGIAWLGc_kIRnukWNy4v0nDXcJ4wEZMBYSgCGhb3XZ6aWr0EeuWrjctVG7wKhD7dto4XxbVxgVqA22Xak9npIjq0uPZ7tzRD5m0_fJczx_fXqZPMxjw8epiAuQVBQZNwkIwxKQGm2S64wLVqRILTU2CzkkAJRJnoOV3IpUam6B5UXKRuRqO3fV1F9r9K1aOm-wLHWF9dorITJgicgCyLegaWrvG7Rq1bilbjoFVPWiVG9B9RaUFGojSonQdrGbv86XWOybdmZCfrnLtTe6tI2ujPN7LGzPKEsCNttiP67E7l-r1Wz6mPRBX5diU-3fc78dhEHqt8NGeeOwMli4Bk2ritr9_aFfFA-V5w</recordid><startdate>19870810</startdate><enddate>19870810</enddate><creator>Vu, Quang A.</creator><creator>Zhang, Dong-er</creator><creator>Chroneos, Zissis C.</creator><creator>Nelson, Daniel A.</creator><general>Elsevier B.V</general><general>Elsevier</general><scope>6I.</scope><scope>AAFTH</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>7X8</scope></search><sort><creationdate>19870810</creationdate><title>Polyamines inhibit the yeast histone deacetylase</title><author>Vu, Quang A. ; Zhang, Dong-er ; Chroneos, Zissis C. ; Nelson, Daniel A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4957-d1807d64c217c3218aef2ba6473d5e0f0cf67d612110384b1f84f758a4f13bd53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>Acetates - metabolism</topic><topic>Amidohydrolases - antagonists & inhibitors</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Biological and medical sciences</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Histone deacetylase</topic><topic>Histone Deacetylase Inhibitors</topic><topic>Hydrolases</topic><topic>Mes, 4-morpholineethanesulfonic acid</topic><topic>n-Butyrate</topic><topic>PMSF, phenylmethylsulfonyl fluoride</topic><topic>Polyamines - pharmacology</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - enzymology</topic><topic>Spermidine</topic><topic>Spermidine - pharmacology</topic><topic>Spermine</topic><topic>Spermine - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Vu, Quang A.</creatorcontrib><creatorcontrib>Zhang, Dong-er</creatorcontrib><creatorcontrib>Chroneos, Zissis C.</creatorcontrib><creatorcontrib>Nelson, Daniel A.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Vu, Quang A.</au><au>Zhang, Dong-er</au><au>Chroneos, Zissis C.</au><au>Nelson, Daniel A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Polyamines inhibit the yeast histone deacetylase</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1987-08-10</date><risdate>1987</risdate><volume>220</volume><issue>1</issue><spage>79</spage><epage>83</epage><pages>79-83</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><coden>FEBLAL</coden><abstract>n-Butyrate inhibits the histone deacetylase from higher cells, but has little effect on the enzyme activity in
Saccharomyces cerevisiae. Spermine and spermidine were therefore tested as potential yeast deacetylase inhibitors and found to inhibit fully the enzyme at 2 and 5 mM, respectively. The utility of these inhibitors was demonstrated by showing that 2 mM spermine substantially increased the incorporation of [
3H]acetate into histone in a yeast nuclear acetyltransferase assay.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><pmid>3301411</pmid><doi>10.1016/0014-5793(87)80879-7</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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source | MEDLINE; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
subjects | Acetates - metabolism Amidohydrolases - antagonists & inhibitors Analytical, structural and metabolic biochemistry Biological and medical sciences Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Histone deacetylase Histone Deacetylase Inhibitors Hydrolases Mes, 4-morpholineethanesulfonic acid n-Butyrate PMSF, phenylmethylsulfonyl fluoride Polyamines - pharmacology Saccharomyces cerevisiae Saccharomyces cerevisiae - enzymology Spermidine Spermidine - pharmacology Spermine Spermine - pharmacology |
title | Polyamines inhibit the yeast histone deacetylase |
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