2byk
Histone fold heterodimer of the Chromatin Accessibility Complex
Structural highlights
FunctionDPOE3_DROME Accessory component of the DNA polymerase epsilon complex (By similarity). Participates in DNA repair and in chromosomal DNA replication (By similarity). Histone-like protein which promotes nucleosome sliding of ATP-dependent nucleosome remodeling complexes (PubMed:10856248, PubMed:11447119, PubMed:18327268). Part of the chromatin-accessibility complex (CHRAC) which uses energy/ATP to increase the general accessibility of DNA in chromatin (PubMed:10856248, PubMed:11447119). As an heterodimer with Chrac-16, binds DNA and facilitates nucleosome sliding by Acf (PubMed:16260604). Has a role in DNA damage response by preventing cid mislocalization to chromatin (PubMed:24703848).[UniProtKB:Q04603][UniProtKB:Q9NRF9][1] [2] [3] [4] [5] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe chromatin accessibility complex (CHRAC) is an abundant, evolutionarily conserved nucleosome remodeling machinery able to catalyze histone octamer sliding on DNA. CHRAC differs from the related ACF complex by the presence of two subunits with molecular masses of 14 and 16 kDa, whose structure and function were not known. We determined the structure of Drosophila melanogaster CHRAC14-CHRAC16 by X-ray crystallography at 2.4-angstroms resolution and found that they dimerize via a variant histone fold in a typical handshake structure. In further analogy to histones, CHRAC14-16 contain unstructured N- and C-terminal tail domains that protrude from the handshake structure. A dimer of CHRAC14-16 can associate with the N terminus of ACF1, thereby completing CHRAC. Low-affinity interactions of CHRAC14-16 with DNA significantly improve the efficiency of nucleosome mobilization by limiting amounts of ACF. Deletion of the negatively charged C terminus of CHRAC16 enhances DNA binding 25-fold but leads to inhibition of nucleosome sliding, in striking analogy to the effect of the DNA chaperone HMGB1 on nucleosome sliding. The presence of a surface compatible with DNA interaction and the geometry of an H2A-H2B heterodimer may provide a transient acceptor site for DNA dislocated from the histone surface and therefore facilitate the nucleosome remodeling process. The histone fold subunits of Drosophila CHRAC facilitate nucleosome sliding through dynamic DNA interactions.,Hartlepp KF, Fernandez-Tornero C, Eberharter A, Grune T, Muller CW, Becker PB Mol Cell Biol. 2005 Nov;25(22):9886-96. PMID:16260604[6] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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