Ontology highlight
ABSTRACT:
SUBMITTER: Liu B
PROVIDER: S-EPMC4343176 | biostudies-literature | 2015 Feb
REPOSITORIES: biostudies-literature
Proceedings of the National Academy of Sciences of the United States of America 20150202 7
RNA polymerase (RNAP) loses activity during transcription as it stalls at various inactive states due to erratic translocation. Reactivation of these stalled RNAPs is essential for efficient RNA synthesis. Here we report a 4.7-Å resolution crystal structure of the Escherichia coli RNAP core enzyme in complex with ATPase RapA that is involved in reactivating stalled RNAPs. The structure reveals that RapA binds at the RNA exit channel of the RNAP and makes the channel unable to accommodate the for ...[more]