Recent structural studies of RNA polymerases II and III.

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 Trans

authors

Cramer P

doi

10.1042/BST0341058

subject

Has Abstract

pub_date

2006-12-01 00:00:00

pages

1058-61

issue

Pt 6

eissn

0300-5127

issn

1470-8752

pii

BST0341058

journal_volume

34

pub_type

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