5VKO

SPT6 tSH2-RPB1 1468-1500 pT1471, pS1493

Summary for 5VKO

• Entry DOI: 10.2210/pdb5vko/pdb
• Related: 5VKL
• Descriptor: Transcription elongation factor SPT6, DNA-directed RNA polymerase II subunit RPB1, ISOPROPYL ALCOHOL, ... (4 entities in total)
• Functional Keywords: sh2 domain phosphorylation histone chaperone transcription, transcription
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); More
• Total number of polymer chains: 2
• Total formula weight: 28803.31

Authors

Sdano, M.A.,Whitby, F.G.,Hill, C.P. (deposition date: 2017-04-21, release date: 2017-09-20, Last modification date: 2024-10-09)

Primary citation

Sdano, M.A.,Fulcher, J.M.,Palani, S.,Chandrasekharan, M.B.,Parnell, T.J.,Whitby, F.G.,Formosa, T.,Hill, C.P.
A novel SH2 recognition mechanism recruits Spt6 to the doubly phosphorylated RNA polymerase II linker at sites of transcription.
Elife, 6:-, 2017

PubMed Abstract: We determined that the tandem SH2 domain of Spt6 binds the linker region of the RNA polymerase II subunit Rpb1 rather than the expected sites in its heptad repeat domain. The 4 nM binding affinity requires phosphorylation at Rpb1 S1493 and either T1471 or Y1473. Crystal structures showed that pT1471 binds the canonical SH2 pY site while pS1493 binds an unanticipated pocket 70 Å distant. Remarkably, the pT1471 phosphate occupies the phosphate-binding site of a canonical pY complex, while Y1473 occupies the position of a canonical pY side chain, with the combination of pT and Y mimicking a pY moiety. Biochemical data and modeling indicate that pY1473 can form an equivalent interaction, and we find that pT1471/pS1493 and pY1473/pS1493 combinations occur in vivo. ChIP-seq and genetic analyses demonstrate the importance of these interactions for recruitment of Spt6 to sites of transcription and for the maintenance of repressive chromatin.

PubMed: 28826505
DOI: 10.7554/eLife.28723

Experimental method

X-RAY DIFFRACTION (1.8 Å)