TAILIEUCHUNG - Báo cáo khoa học: Site specificity of yeast histone acetyltransferase B complex in vivo

Saccharomyces cerevisiaeHat1, together with Hat2 and Hif1, forms the his-tone acetyltransferase B (HAT-B) complex. Previous studies performed with synthetic N-terminal histone H4 peptides found that whereas the HAT-B complex acetylates only Lys12, recombinant Hat1 is able to modify Lys12 and Lys5. | ễFEBS Journal Site specificity of yeast histone acetyltransferase B complex in vivo Ana Poveda and Ramon Sendra Departament de Bioquimica i Biologia Molecular Universitat de Valencia Spain Keywords acetylation acetyltransferase chromatin histones yeast Correspondence R. Sendra Departament de Bioquimica i Biologia Molecular Facultat de Ciencies Biologiques C Dr Moliner 50 46100-Burjassot Valencia Spain Fax 34 96 354 4635 Tel 34 96 354 3015 E-mail Present address IGH-Institute of Human Genetics CNRS Montpellier France Received 25 January 2008 revised 25 February 2008 accepted 28 February 2008 doi Saccharomyces cerevisiae Hatl together with Hat2 and Hif1 forms the histone acetyltransferase B HAT-B complex. Previous studies performed with synthetic N-terminal histone H4 peptides found that whereas the HAT-B complex acetylates only Lys12 recombinant Hat1 is able to modify Lys12 and Lys5. Here we demonstrate that both Lys12 and Lys5 of soluble non-chromatin-bound histone H4 are in vivo targets of acetylation for the yeast HAT-B enzyme. Moreover coimmunoprecipitation assays revealed that Lys12 Lys5-acetylated histone H4 is bound to the HAT-B complex in the soluble cell fraction. Both Hat1 and Hat2 but not Hif1 are required for the Lys12 Lys5-specific acetylation and for histone H4 binding. HAT-B-dependent acetylation of histone H4 was detected in the soluble fraction of cells at distinct cell cycle stages and increased when cells accumulated excess histones. Strikingly histone H3 was not found in any of the immunoprecipitates obtained with the different components of the HAT-B enzyme indicating the possibility that histone H3 is not together with histone H4 in this complex. Finally the exchange of Lys for Arg at position 12 of histone H4 did not interfere with histone H4 association with the complex but prevented acetylation on Lys5 by the HAT-B enzyme in vivo as well as in vitro. Histone acetylation is a highly dynamic

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