Abstract：
:Transcriptional pausing by multisubunit RNA polymerases (RNAPs) is a key mechanism for regulating gene expression in both prokaryotes and eukaryotes and is a prerequisite for transcription termination. Pausing and termination states are thought to arise through a common, elemental pause state that is inhibitory for nucleotide addition. We report three crystal structures of Thermus RNAP elemental paused elongation complexes (ePECs). The structures reveal the same relaxed, open-clamp RNAP conformation in the ePEC that may arise by failure to re-establish DNA contacts during translocation. A kinked bridge-helix sterically blocks the RNAP active site, explaining how this conformation inhibits RNAP catalytic activity. Our results provide a framework for understanding how RNA hairpin formation stabilizes the paused state and how the ePEC intermediate facilitates termination.
journal_name
Celljournal_title
Cellauthors
Weixlbaumer A,Leon K,Landick R,Darst SAdoi
10.1016/j.cell.2012.12.020subject
Has Abstractpub_date
2013-01-31 00:00:00pages
431-41issue
3eissn
0092-8674issn
1097-4172pii
S0092-8674(12)01542-5journal_volume
152pub_type
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