Structural highlights
Function
[SPT6_CANGA] Plays a role in maintenance of chromatin structure during RNA polymerase II transcription elongation thereby repressing transcription initiation from cryptic promoters. Mediates the reassembly of nucleosomes onto the promoters of at least a selected set of genes during repression; the nucleosome reassembly is essential for transcriptional repression (By similarity).
Publication Abstract from PubMed
Spt6 is an essential transcription elongation factor and histone chaperone that binds the C-terminal repeat domain (CTD) of RNA polymerase (Pol) II. We show here that Spt6 contains a tandem SH2 domain with a novel structure and CTD-binding mode. The tandem SH2 domain binds to a serine 2-phosphorylated CTD peptide in vitro, whereas its N-terminal SH2 subdomain, which we previously characterized, does not. CTD binding requires a positively charged crevice in the C-terminal SH2 subdomain, which lacks the canonical phospho-binding pocket of SH2 domains and had previously escaped detection. The tandem SH2 domain is apparently required for transcription elongation in vivo, as its deletion in cells is lethal in the presence of 6-azauracil.
A tandem SH2 domain in transcription elongation factor Spt6 binds the phosphorylated RNA polymerase II CTD.,Sun M, Lariviere L, Dengl S, Mayer A, Cramer P J Biol Chem. 2010 Oct 6. PMID:20926372[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sun M, Lariviere L, Dengl S, Mayer A, Cramer P. A tandem SH2 domain in transcription elongation factor Spt6 binds the phosphorylated RNA polymerase II CTD. J Biol Chem. 2010 Oct 6. PMID:20926372 doi:10.1074/jbc.M110.144568
