Histone H4 lysine 91 acetylation a core domain modification associated with chromatin assembly. Export

@article{citeulike:4683702, abstract = {The acetylation of the NH2-terminal tail of histone H4 by type B histone acetyltransferases (HATs) is involved in the process of chromatin assembly. Histone H4 associated with a nuclear type B HAT complex contains modifications in its globular core domain as well. In particular, acetylation was found at lysine 91. A mutation that alters this residue, which lies in the interface between histone H3/H4 tetramers and H2A/H2B dimers, confers phenotypes consistent with defects in chromatin assembly such as sensitivity to DNA damaging agents and derepression and alteration of silent chromatin structure. In addition, this mutation destabilizes the histone octamer, leading to defects in chromatin structure. These results indicate an important role for histone modifications outside the NH2-tail domains in the processes of chromatin assembly, DNA repair, and transcriptional silencing.}, author = {Ye, J. and Ai, X. and Eugeni, E. E. and Zhang, L. and Carpenter, L. R. and Jelinek, M. A. and Freitas, M. A. and Parthun, M. R.}, citeulike-article-id = {4683702}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/j.molcel.2005.02.031}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/15808514}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=15808514}, day = {1}, doi = {10.1016/j.molcel.2005.02.031}, issn = {1097-2765}, journal = {Molecular cell}, keywords = {histone\_acetylation, nucleosome, nucleosome\_assembly}, month = {April}, number = {1}, pages = {123--130}, posted-at = {2009-05-31 00:06:24}, priority = {2}, title = {Histone H4 lysine 91 acetylation a core domain modification associated with chromatin assembly.}, url = {http://dx.doi.org/10.1016/j.molcel.2005.02.031}, volume = {18}, year = {2005} }

TY - JOUR ID - citeulike:4683702 L3 - citeulike-article-id:4683702 N2 - The acetylation of the NH2-terminal tail of histone H4 by type B histone acetyltransferases (HATs) is involved in the process of chromatin assembly. Histone H4 associated with a nuclear type B HAT complex contains modifications in its globular core domain as well. In particular, acetylation was found at lysine 91. A mutation that alters this residue, which lies in the interface between histone H3/H4 tetramers and H2A/H2B dimers, confers phenotypes consistent with defects in chromatin assembly such as sensitivity to DNA damaging agents and derepression and alteration of silent chromatin structure. In addition, this mutation destabilizes the histone octamer, leading to defects in chromatin structure. These results indicate an important role for histone modifications outside the NH2-tail domains in the processes of chromatin assembly, DNA repair, and transcriptional silencing. IS - 1 JF - Molecular cell SN - 1097-2765 EP - 130 TI - Histone H4 lysine 91 acetylation a core domain modification associated with chromatin assembly. VL - 18 SP - 123 KW - histone_acetylation KW - nucleosome KW - nucleosome_assembly AU - Ye, J AU - Ai, X AU - Eugeni, EE AU - Zhang, L AU - Carpenter, LR AU - Jelinek, MA AU - Freitas, MA AU - Parthun, MR PY - 2005/04/01/ UR - http://dx.doi.org/10.1016/j.molcel.2005.02.031 ER -