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Structure of THE RNA POLYMERASE LAMBDA-BASED ANTITERMINATION COMPLEXStructure of THE RNA POLYMERASE LAMBDA-BASED ANTITERMINATION COMPLEX
Structural highlights
FunctionNUSA_ECOLI Participates in both transcription termination and antitermination. Involved in a variety of cellular and viral termination and antitermination processes, such as Rho-dependent transcriptional termination, intrinsic termination, and phage lambda N-mediated transcriptional antitermination. Also important for coordinating the cellular responses to DNA damage by coupling the processes of nucleotide excision repair and translesion synthesis to transcription.[1] [2] [3] [4] [5] [6] [7] [8] [9] Publication Abstract from PubMedBacteriophage lambdaN protein, a model anti-termination factor, binds nascent RNA and host Nus factors, rendering RNA polymerase resistant to all pause and termination signals. A 3.7-A-resolution cryo-electron microscopy structure and structure-informed functional analyses reveal a multi-pronged strategy by which the intrinsically unstructured lambdaN directly modifies RNA polymerase interactions with the nucleic acids and subverts essential functions of NusA, NusE, and NusG to reprogram the transcriptional apparatus. lambdaN repositions NusA and remodels the beta subunit flap tip, which likely precludes folding of pause or termination RNA hairpins in the exit tunnel and disrupts termination-supporting interactions of the alpha subunit C-terminal domains. lambdaN invades and traverses the RNA polymerase hybrid cavity, likely stabilizing the hybrid and impeding pause- or termination-related conformational changes of polymerase. lambdaN also lines upstream DNA, seemingly reinforcing anti-backtracking and anti-swiveling by NusG. Moreover, lambdaN-repositioned NusA and NusE sequester the NusG C-terminal domain, counteracting rho-dependent termination. Other anti-terminators likely utilize similar mechanisms to enable processive transcription. Structural Basis for the Action of an All-Purpose Transcription Anti-termination Factor.,Krupp F, Said N, Huang YH, Loll B, Burger J, Mielke T, Spahn CMT, Wahl MC Mol Cell. 2019 Feb 12. pii: S1097-2765(19)30036-X. doi:, 10.1016/j.molcel.2019.01.016. PMID:30795892[10] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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