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Site-specificity of pea histone acetyltransferase B in vitro

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Site-specificity of pea histone acetyltransferase B in vitro

dc.contributor.author	Mingarro Muñoz, Ismael
dc.contributor.author	Sendra Pérez, Ramón
dc.contributor.author	Salvador Alcober, María Luisa
dc.contributor.author	Franco Vera, Luis
dc.date.accessioned	2016-09-06T18:22:13Z
dc.date.available	2016-09-06T18:22:13Z
dc.date.issued	1993
dc.identifier.citation	Mingarro Muñoz, Ismael Sendra Pérez, Ramón Salvador Alcober, María Luisa Franco Vera, Luis 1993 Site-specificity of pea histone acetyltransferase B in vitro Journal of Biological Chemistry 268 18 13248 13252
dc.identifier.uri	http://hdl.handle.net/10550/54929
dc.description.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.
dc.language.iso	eng
dc.relation.ispartof	Journal of Biological Chemistry, 1993, vol. 268, num. 18, p. 13248-13252
dc.subject	Proteïnes
dc.subject	Bioquímica
dc.title	Site-specificity of pea histone acetyltransferase B in vitro
dc.type	journal article	es_ES
dc.date.updated	2016-09-06T18:22:14Z
dc.identifier.doi	http://www.jbc.org/content/268/18/13248
dc.identifier.idgrec	003209
dc.rights.accessRights	open access	es_ES