Structural highlights
Function
EP400_HUMAN Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. May be required for transcriptional activation of E2F1 and MYC target genes during cellular proliferation. The NuA4 complex ATPase and helicase activities seem to be, at least in part, contributed by the association of RUVBL1 and RUVBL2 with EP400. May regulate ZNF42 transcription activity. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AZ1 from the nucleosome.[1] [2] DHAA_PSEPV Catalyzes hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons. Has a broad substrate specificity, as it is able to dehalogenate mono- and di- chlorinated and brominated alkanes (up to at least C10), and the two isomers of 1,3-dichloropropene to 3-chloroallyl alcohol; the highest activity was found with 1,2-dibromoethane, while no activity was observed with the analog 1,2-dichloroethane.[3]
References
- ↑ Doyon Y, Selleck W, Lane WS, Tan S, Cote J. Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans. Mol Cell Biol. 2004 Mar;24(5):1884-96. PMID:14966270
- ↑ Obri A, Ouararhni K, Papin C, Diebold ML, Padmanabhan K, Marek M, Stoll I, Roy L, Reilly PT, Mak TW, Dimitrov S, Romier C, Hamiche A. ANP32E is a histone chaperone that removes H2A.Z from chromatin. Nature. 2014 Jan 30;505(7485):648-53. doi: 10.1038/nature12922. Epub 2014 Jan 22. PMID:24463511 doi:http://dx.doi.org/10.1038/nature12922
- ↑ Poelarends GJ, Wilkens M, Larkin MJ, van Elsas JD, Janssen DB. Degradation of 1,3-dichloropropene by pseudomonas cichorii 170. Appl Environ Microbiol. 1998 Aug;64(8):2931-6. PMID:9687453 doi:10.1128/AEM.64.8.2931-2936.1998
