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H3R42me2a is a histone modification with positive transcriptional effects

Author(s): Casadio, Fabio; Lu, Xiangdong; Pollock, Samuel B.; LeRoy, Gary; Garcia, Benjamin A.; et al

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dc.contributor.authorCasadio, Fabio-
dc.contributor.authorLu, Xiangdong-
dc.contributor.authorPollock, Samuel B.-
dc.contributor.authorLeRoy, Gary-
dc.contributor.authorGarcia, Benjamin A.-
dc.contributor.authorMuir, Thomas W.-
dc.contributor.authorRoeder, Robert G.-
dc.contributor.authorAllis, C. David-
dc.date.accessioned2020-10-30T18:52:09Z-
dc.date.available2020-10-30T18:52:09Z-
dc.date.issued2013-09-10en_US
dc.identifier.citationCasadio, F., Lu, X., Pollock, S.B., LeRoy, G., Garcia, B.A., Muir, T.W., Roeder, R.G., Allis, C.D. (2013). H3R42me2a is a histone modification with positive transcriptional effects. Proceedings of the National Academy of Sciences, 110 (37), 14894 - 14899. doi:10.1073/pnas.1312925110en_US
dc.identifier.issn0027-8424-
dc.identifier.urihttp://arks.princeton.edu/ark:/88435/pr1680t-
dc.descriptionProceedings of the National Academy of Sciences of the United States of America Volume 110, Issue 37, 10 September 2013, Pages 14894-14899. Authors: Fabio Casadio, Xiangdong Lu, Samuel B. Pollock, Gary LeRoy, Benjamin A. Garcia, Thomas W. Muir (Tom W. Muir), Robert G. Roeder, and C. David Allis,en_US
dc.description.abstractHistone posttranslational modification leads to downstream effects indirectly by allowing or preventing docking of effector molecules, or directly by changing the intrinsic biophysical properties of local chromatin. To date, little has been done to study posttranslational modifications that lie outside of the unstructured tail domains of histones. Core residues, and in particular arginines in H3 and H4, mediate key interactions between the histone octamer and DNA in forming the nucleosomal particle. Using mass spectrometry, we find that one of these core residues, arginine 42 of histone H3 (H3R42), is dimethylated in mammalian cells by the methyltransferases coactivator arginine methyltransferase 1 (CARM1) and protein arginine methyltransferase 6 (PRMT6) in vitro and in vivo, and we demonstrate that methylation of H3R42 stimulates transcription in vitro from chromatinized templates. Thus, H3R42 is a new, "nontail" histone methylation site with positive effects on transcription. We propose that methylation of basic histone residues at the DNA interface may disrupt histone:DNA interactions, with effects on downstream processes, notably transcription.en_US
dc.format.extent110.37:14894 - 14899en_US
dc.language.isoen_USen_US
dc.relation.ispartofProceedings of the National Academy of Sciencesen_US
dc.rightsFinal published version. This is an open access article.en_US
dc.titleH3R42me2a is a histone modification with positive transcriptional effectsen_US
dc.typeJournal Articleen_US
dc.identifier.doidoi:10.1073/pnas.1312925110-
dc.date.eissued2013-08-26en_US
dc.identifier.eissn1091-6490-
pu.type.symplectichttp://www.symplectic.co.uk/publications/atom-terms/1.0/journal-articleen_US

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