InterPro domain: IPR017072

Spt6 is an essential histone chaperone that mediates nucleosome reassembly during gene transcription. The N-terminal ~300 residues are highly acidic, predicted to be disordered, and are necessary for binding both nucleosomes and the transcription factor Spn1/IWS1 [ 1 ]. Spt6 associates with RNAPII via a tandem Src2 homology domain [ 2 , 3 ]. Spt6-RNAPII association is required for efficient recruitment of the Ccr4-Not de-adenylation complex to transcribed genes for mRNA turnover [ 4 ]. Spt6 has a key function in transcription elongation. In yeast, Spt6's interaction with phosphorylated tyrosine 1 at the C-terminal domain of RNAPII prevents pre-mature recruitment of termination factors to genes [ 5 ].

1. Structure and biological importance of the Spn1-Spt6 interaction, and its regulatory role in nucleosome binding. Mol. Cell 40, 725-35
2. Noncanonical tandem SH2 enables interaction of elongation factor Spt6 with RNA polymerase II. J. Biol. Chem. 285, 38389-98
3. A novel SH2 recognition mechanism recruits Spt6 to the doubly phosphorylated RNA polymerase II linker at sites of transcription. Elife 6, 1723-5
4. Spt6 Association with RNA Polymerase II Directs mRNA Turnover During Transcription. Mol. Cell 70, 1054-1066.e4
5. CTD tyrosine phosphorylation impairs termination factor recruitment to RNA polymerase II. Science 336