Structural highlights
Publication Abstract from PubMed
The activity of RNA polymerase II (Pol II) is controlled in part by the phosphorylation state of the C-terminal domain (CTD) of its largest subunit. Recent reports have suggested that yeast regulator of transcription protein, Rtr1, and its human homologue RPAP2, possess Pol II CTD Ser5 phosphatase activity. Here we report the crystal structure of Kluyveromyces lactis Rtr1, which reveals a new type of zinc finger protein and does not have any close structural homologues. Importantly, the structure does not show evidence of an active site, and extensive experiments to demonstrate its CTD phosphatase activity have been unsuccessful, suggesting that Rtr1 has a non-catalytic role in CTD dephosphorylation.
The yeast regulator of transcription protein Rtr1 lacks an active site and phosphatase activity.,Xiang K, Manley JL, Tong L Nat Commun. 2012 Jul 10;3:946. doi: 10.1038/ncomms1947. PMID:22781759[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Xiang K, Manley JL, Tong L. The yeast regulator of transcription protein Rtr1 lacks an active site and phosphatase activity. Nat Commun. 2012 Jul 10;3:946. doi: 10.1038/ncomms1947. PMID:22781759 doi:10.1038/ncomms1947
