Acetylation by Tip60 is required for selective histone variant exchange at DNA lesions.

@article{citeulike:2120371, abstract = {Phosphorylation of the human histone variant H2A.X and H2Av, its homolog in Drosophila melanogaster, occurs rapidly at sites of DNA double-strand breaks. Little is known about the function of this phosphorylation or its removal during DNA repair. Here, we demonstrate that the Drosophila Tip60 (dTip60) chromatin-remodeling complex acetylates nucleosomal phospho-H2Av and exchanges it with an unmodified H2Av. Both the histone acetyltransferase dTip60 as well as the adenosine triphosphatase Domino/p400 catalyze the exchange of phospho-H2Av. Thus, these data reveal a previously unknown mechanism for selective histone exchange that uses the concerted action of two distinct chromatin-remodeling enzymes within the same multiprotein complex.}, address = {Stowers Institute for Medical Research, 1000 East 50th Street, Kansas City, MO 64110, USA. tnk@stowers-institute.org}, author = {Kusch, T. and Florens, L. and Macdonald, W. H. and Swanson, S. K. and Glaser, R. L. and Yates, J. R. and Abmayr, S. M. and Washburn, M. P. and Workman, J. L. }, citeulike-article-id = {2120371}, doi = {http://dx.doi.org/10.1126/science.1103455}, issn = {1095-9203}, journal = {Science}, keywords = {chromatin, chromatin-remodeling-modification, dna-damage, drosophila, h2a, h2av, tip60}, month = {December}, number = {5704}, pages = {2084--2087}, posted-at = {2007-12-14 20:33:50}, priority = {2}, title = {Acetylation by Tip60 is required for selective histone variant exchange at DNA lesions.}, url = {http://dx.doi.org/10.1126/science.1103455}, volume = {306}, year = {2004} }

TY - JOUR ID - citeulike:2120371 L3 - citeulike-article-id:2120371 TI - Acetylation by Tip60 is required for selective histone variant exchange at DNA lesions. JF - Science VL - 306 IS - 5704 SP - 2084 EP - 2087 AD - Stowers Institute for Medical Research, 1000 East 50th Street, Kansas City, MO 64110, USA. tnk@stowers-institute.org SN - 1095-9203 N2 - Phosphorylation of the human histone variant H2A.X and H2Av, its homolog in Drosophila melanogaster, occurs rapidly at sites of DNA double-strand breaks. Little is known about the function of this phosphorylation or its removal during DNA repair. Here, we demonstrate that the Drosophila Tip60 (dTip60) chromatin-remodeling complex acetylates nucleosomal phospho-H2Av and exchanges it with an unmodified H2Av. Both the histone acetyltransferase dTip60 as well as the adenosine triphosphatase Domino/p400 catalyze the exchange of phospho-H2Av. Thus, these data reveal a previously unknown mechanism for selective histone exchange that uses the concerted action of two distinct chromatin-remodeling enzymes within the same multiprotein complex. KW - chromatin KW - chromatin-remodeling-modification KW - dna-damage KW - drosophila KW - h2a KW - h2av KW - tip60 AU - Kusch, T AU - Florens, L AU - Macdonald, WH AU - Swanson, SK AU - Glaser, RL AU - Yates, JR AU - Abmayr, SM AU - Washburn, MP AU - Workman, JL PY - 2004/12/17/ UR - http://dx.doi.org/10.1126/science.1103455 ER -