Yeast Rtt109 promotes genome stability by acetylating histone H3 on lysine 56

Science

Volumn 315, Issue 5812, 2007, Pages 649-652

  Driscoll, Robert ^a   Hudson, Amanda ^a   Jackson, Stephen P ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; DNA; HISTONE H3; LYSINE;

AMINO ACID; CHEMICAL REACTION; DNA; ENZYME ACTIVITY; GENOME; YEAST;

ACETYLATION; ARTICLE; CELL CYCLE; CELL CYCLE S PHASE; CELL SURVIVAL; CHROMATIN STRUCTURE; DNA DAMAGE; FLOW CYTOMETRY; GENOMIC INSTABILITY; NONHUMAN; PRIORITY JOURNAL; SACCHAROMYCES CEREVISIAE; YEAST; YEAST CELL;

ACETYLATION; CELL CYCLE PROTEINS; CHROMOSOMES, FUNGAL; DNA BREAKS, DOUBLE-STRANDED; DNA DAMAGE; GENOME, FUNGAL; GENOMIC INSTABILITY; HISTONE ACETYLTRANSFERASES; HISTONES; LYSINE; MUTATION; RECOMBINANT PROTEINS; S PHASE; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SUBSTRATE SPECIFICITY;

SACCHAROMYCES CEREVISIAE;

EID: 33846818840     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1135862     Document Type: Article

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21. We thank A. Aguilera, M. Lisby, R. Rothstein, D. P. Toczyski, Z. Zhang, P. D. Kaufman, T. Bartke, and N. Lowndes for strains and reagents and S. Gravel, P. Huertas, A. Bannister, and T. Kouzarides for technical advice and critical reading of the manuscript. R.D. is supported by a U.K. Biotechnology and Biological Sciences Research Council (BBSRC) Cooperative Awards in Science and Engineering (CASE) studentship with KuDOS Pharmaceuticals and by a Cancer Research UK programme grant to S.P.J. Research in the S.P.J. laboratory is made possible by core infrastructure funding from Cancer Research UK and the Wellcome Trust.