title: Genome integrity: a HAT needs a chaperone.
abstract: Histone acetylation helps to maintain integrity of the yeast replisome in response to genotoxic agents. Four groups have now identified protein Rtt109p as the catalytic subunit of a novel histone H3 acetylase complex that harbors a histone chaperone subunit essential for significant activity.
authors.affiliation: Program in Molecular Medicine, University of Massachusetts Medical School, Worcester, Massachusetts 01605, USA. craig.peterson@umassmed.edu
authors.forename: Craig L
authors.initials: CL
authors.lastname: Peterson
mesh_terms: D004260:DNA Repair; D042822:Genomic Instability / Q000235:genetics*; D051548:Histone Acetyltransferases / Q000378:metabolism*; D006657:Histones / Q000235:genetics / Q000378:metabolism*; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000235:genetics*; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism*
chemical_list: D006657:Histones; D018832:Molecular Chaperones; D029701:Saccharomyces cerevisiae Proteins; D051548:Histone Acetyltransferases; C517120:Rtt109 protein, S cerevisiae