Abstract:
:Here, I review three new structural studies from our laboratory. First, the crystal structure of RNA polymerase (Pol) II in complex with an RNA inhibitor revealed that this RNA blocks transcription initiation by preventing DNA loading into the active-centre cleft. Secondly, the structure of the SRI (Set2 Rpb1-interacting) domain of the histone methyltransferase Set2 revealed a novel fold for specific interaction with the doubly phosphorylated CTD (C-terminal repeat domain) of Pol II. Finally, we obtained the first structural information on Pol III, in the form of an 11-subunit model obtained by combining a homology model of the nine-subunit core enzyme with a new X-ray structure of the subcomplex C17/25.
journal_name
Biochem Soc Transjournal_title
Biochemical Society transactionsauthors
Cramer Pdoi
10.1042/BST0341058subject
Has Abstractpub_date
2006-12-01 00:00:00pages
1058-61issue
Pt 6eissn
0300-5127issn
1470-8752pii
BST0341058journal_volume
34pub_type
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