CBP/p300-mediated acetylation of histone H3 on lysine 56 Export

@article{citeulike:4153145, abstract = {Acetylation within the globular core domain of histone H3 on lysine 56 (H3K56) has recently been shown to have a critical role in packaging DNA into chromatin following DNA replication and repair in budding yeast. However, the function or occurrence of this specific histone mark has not been studied in multicellular eukaryotes, mainly because the Rtt109 enzyme that is known to mediate acetylation of H3K56 (H3K56ac) is fungal-specific. Here we demonstrate that the histone acetyl transferase CBP (also known as Nejire) in flies and CBP and p300 (Ep300) in humans acetylate H3K56, whereas Drosophila Sir2 and human SIRT1 and SIRT2 deacetylate H3K56ac. The histone chaperones ASF1A in humans and Asf1 in Drosophila are required for acetylation of H3K56 in vivo, whereas the histone chaperone CAF-1 (chromatin assembly factor 1) in humans and Caf1 in Drosophila are required for the incorporation of histones bearing this mark into chromatin. We show that, in response to DNA damage, histones bearing acetylated K56 are assembled into chromatin in Drosophila and human cells, forming foci that colocalize with sites of DNA repair. Furthermore, acetylation of H3K56 is increased in multiple types of cancer, correlating with increased levels of ASF1A in these tumours. Our identification of multiple proteins regulating the levels of H3K56 acetylation in metazoans will allow future studies of this critical and unique histone modification that couples chromatin assembly to DNA synthesis, cell proliferation and cancer.}, author = {Das, Chandrima and Lucia, M. Scott and Hansen, Kirk C. and Tyler, Jessica K.}, citeulike-article-id = {4153145}, citeulike-linkout-0 = {http://dx.doi.org/10.1038/nature07861}, citeulike-linkout-1 = {http://dx.doi.org/10.1038/nature07861}, citeulike-linkout-2 = {http://view.ncbi.nlm.nih.gov/pubmed/19270680}, citeulike-linkout-3 = {http://www.hubmed.org/display.cgi?uids=19270680}, day = {7}, doi = {10.1038/nature07861}, issn = {0028-0836}, journal = {Nature}, keywords = {h3k56}, month = {May}, number = {7243}, pages = {113--117}, posted-at = {2009-03-22 14:24:35}, priority = {2}, publisher = {Macmillan Publishers Limited. All rights reserved}, title = {CBP/p300-mediated acetylation of histone H3 on lysine 56}, url = {http://dx.doi.org/10.1038/nature07861}, volume = {459}, year = {2009} }

TY - JOUR ID - citeulike:4153145 L3 - citeulike-article-id:4153145 N2 - Acetylation within the globular core domain of histone H3 on lysine 56 (H3K56) has recently been shown to have a critical role in packaging DNA into chromatin following DNA replication and repair in budding yeast. However, the function or occurrence of this specific histone mark has not been studied in multicellular eukaryotes, mainly because the Rtt109 enzyme that is known to mediate acetylation of H3K56 (H3K56ac) is fungal-specific. Here we demonstrate that the histone acetyl transferase CBP (also known as Nejire) in flies and CBP and p300 (Ep300) in humans acetylate H3K56, whereas Drosophila Sir2 and human SIRT1 and SIRT2 deacetylate H3K56ac. The histone chaperones ASF1A in humans and Asf1 in Drosophila are required for acetylation of H3K56 in vivo, whereas the histone chaperone CAF-1 (chromatin assembly factor 1) in humans and Caf1 in Drosophila are required for the incorporation of histones bearing this mark into chromatin. We show that, in response to DNA damage, histones bearing acetylated K56 are assembled into chromatin in Drosophila and human cells, forming foci that colocalize with sites of DNA repair. Furthermore, acetylation of H3K56 is increased in multiple types of cancer, correlating with increased levels of ASF1A in these tumours. Our identification of multiple proteins regulating the levels of H3K56 acetylation in metazoans will allow future studies of this critical and unique histone modification that couples chromatin assembly to DNA synthesis, cell proliferation and cancer. IS - 7243 JF - Nature SN - 0028-0836 EP - 117 TI - CBP/p300-mediated acetylation of histone H3 on lysine 56 PB - Macmillan Publishers Limited. All rights reserved VL - 459 SP - 113 KW - h3k56 AU - Das, Chandrima AU - Lucia, Scott AU - Hansen, Kirk AU - Tyler, Jessica PY - 2009/05/07/ UR - http://dx.doi.org/10.1038/nature07861 ER -