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PMID:23980157

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Citation

Casadio, F, Lu, X, Pollock, SB, Leroy, G, Garcia, BA, Muir, TW, Roeder, RG and Allis, CD (2013) H3R42me2a is a histone modification with positive transcriptional effects. Proc. Natl. Acad. Sci. U.S.A. 110:14894-9

Abstract

Histone 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.

Links

PubMed Online version:10.1073/pnas.1312925110

Keywords


Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

HUMAN:ANM6

GO:0008469: histone-arginine N-methyltransferase activity

ECO:0000314:

F

Figure 2

complete
CACAO 8577

HUMAN:ANM6

enables

GO:0008469: histone-arginine N-methyltransferase activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

HUMAN:CARM1

GO:0008469: histone-arginine N-methyltransferase activity

ECO:0000314:

F

Figure 2

complete
CACAO 8576

HUMAN:CARM1

enables

GO:0008469: histone-arginine N-methyltransferase activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

See also

References

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