Abstract：
:The RNA polymerase elongation complex (EC) is both highly stable and processive, rapidly extending RNA chains for thousands of nucleotides. Understanding the mechanisms of elongation and its regulation requires detailed information about the structural organization of the EC. Here we report the 2.5-A resolution structure of the Thermus thermophilus EC; the structure reveals the post-translocated intermediate with the DNA template in the active site available for pairing with the substrate. DNA strand separation occurs one position downstream of the active site, implying that only one substrate at a time can specifically bind to the EC. The upstream edge of the RNA/DNA hybrid stacks on the beta'-subunit 'lid' loop, whereas the first displaced RNA base is trapped within a protein pocket, suggesting a mechanism for RNA displacement. The RNA is threaded through the RNA exit channel, where it adopts a conformation mimicking that of a single strand within a double helix, providing insight into a mechanism for hairpin-dependent pausing and termination.
journal_name
Naturejournal_title
Natureauthors
Vassylyev DG,Vassylyeva MN,Perederina A,Tahirov TH,Artsimovitch Idoi
10.1038/nature05932subject
Has Abstractpub_date
2007-07-12 00:00:00pages
157-62issue
7150eissn
0028-0836issn
1476-4687pii
nature05932journal_volume
448pub_type
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