Structural highlights
Warning: this is a large structure, and loading might take a long time or not happen at all.
Function
[K0BU55_ECO1E] Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.[HAMAP-Rule:MF_00366][SAAS:SAAS00054255] [B1X6E7_ECODH] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[HAMAP-Rule:MF_00059] [K0BCS5_ECO1E] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[HAMAP-Rule:MF_01322][SAAS:SAAS00054030] [K0AVA1_ECO1C] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[HAMAP-Rule:MF_01321][RuleBase:RU000432] [RAPA_ECOLI] Transcription regulator that activates transcription by stimulating RNA polymerase (RNAP) recycling in case of stress conditions such as supercoiled DNA or high salt concentrations. Probably acts by releasing the RNAP, when it is trapped or immobilized on tightly supercoiled DNA. Does not activate transcription on linear DNA. Probably not involved in DNA repair (By similarity).[1]
Publication Abstract from PubMed
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-A 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 formation of an RNA hairpin. The orientation of RapA on the RNAP core complex suggests that RapA uses its ATPase activity to propel backward translocation of RNAP along the DNA template in an elongation complex. This structure provides insights into the reactivation of stalled RNA polymerases and helps support ATP-driven backward translocation as a general mechanism for transcriptional regulation.
Structural basis for transcription reactivation by RapA.,Liu B, Zuo Y, Steitz TA Proc Natl Acad Sci U S A. 2015 Feb 2. pii: 201417152. PMID:25646438[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sukhodolets MV, Cabrera JE, Zhi H, Jin DJ. RapA, a bacterial homolog of SWI2/SNF2, stimulates RNA polymerase recycling in transcription. Genes Dev. 2001 Dec 15;15(24):3330-41. PMID:11751638 doi:http://dx.doi.org/10.1101/gad.936701
- ↑ Liu B, Zuo Y, Steitz TA. Structural basis for transcription reactivation by RapA. Proc Natl Acad Sci U S A. 2015 Feb 2. pii: 201417152. PMID:25646438 doi:http://dx.doi.org/10.1073/pnas.1417152112
