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Transcription Elongation links to Histone Methylation
Author(s) -
Jones Katherine A,
Bres Vanessa,
Zhang Lirong
Publication year - 2010
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.24.1_supplement.406.2
Subject(s) - p tefb , rna polymerase ii , elongation factor , histone methylation , microbiology and biotechnology , transcription (linguistics) , histone methyltransferase , biology , rna splicing , histone , histone h3 , chemistry , promoter , gene expression , dna methylation , genetics , gene , rna , ribosome , linguistics , philosophy
Many steps in gene expression and mRNA biosynthesis are coupled to transcription elongation. The P‐TEF‐b complex (CycT1:CDK9) overcomes a block to transcription elongation established by the negative‐acting elongation factors, DSIF and NELF. In addition, P‐TEFb phosphorylates the RNAPII CTD, which loads complexes involved in cotranscriptional mRNA processing, surveillance, export, and histone H3K36 methylation. We recently showed that P‐TEFb associates with an alternative splicing factor, SKIP/SNW1, which is required for HIV‐1 Tat transactivation, and will discuss how SKIP stimulates transcription elongation and histone H3K4 methylation at the viral promoter. Thus communication between transcription and splicing occurs in both directions, as the SKIP splicing protein plays a direct role in transcription elongation and H3K4 methylation. We recently reported that Spt6, a transcription elongation factor and histone H3 chaperone, binds directly to the P‐TEFb‐phosphorylated RNAPII CTD to recruit factors to the elongation complex. This megacomplex includes the Hypb/Setd2 histone methyltransferase, which is a CTD‐interacting enzyme that directs H3K36me3 to the coding region of active genes. The assembly of this complex depends upon P‐TEFb activity and is strongly up‐regulated in activated T cells.