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TitleStructural Basis for the Action of an All-Purpose Transcription Anti-termination Factor.
Journal, issue, pagesMol Cell, Vol. 74, Issue 1, Page 143-157.e5, Year 2019
Publish dateApr 4, 2019
AuthorsFerdinand Krupp / Nelly Said / Yong-Heng Huang / Bernhard Loll / Jörg Bürger / Thorsten Mielke / Christian M T Spahn / Markus C Wahl /
PubMed AbstractBacteriophage λN 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-Å-resolution cryo- ...Bacteriophage λN 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-Å-resolution cryo-electron microscopy structure and structure-informed functional analyses reveal a multi-pronged strategy by which the intrinsically unstructured λN directly modifies RNA polymerase interactions with the nucleic acids and subverts essential functions of NusA, NusE, and NusG to reprogram the transcriptional apparatus. λN repositions NusA and remodels the β subunit flap tip, which likely precludes folding of pause or termination RNA hairpins in the exit tunnel and disrupts termination-supporting interactions of the α subunit C-terminal domains. λN invades and traverses the RNA polymerase hybrid cavity, likely stabilizing the hybrid and impeding pause- or termination-related conformational changes of polymerase. λN also lines upstream DNA, seemingly reinforcing anti-backtracking and anti-swiveling by NusG. Moreover, λN-repositioned NusA and NusE sequester the NusG C-terminal domain, counteracting ρ-dependent termination. Other anti-terminators likely utilize similar mechanisms to enable processive transcription.
External linksMol Cell / PubMed:30795892
MethodsEM (single particle)
Resolution3.7 Å
Structure data

0043

6gov

EMDB-0043: cryoEM structure of the lambdaN Transcription Antitermination Complex at 3.7 A resolution.
PDB-6gov: Structure of THE RNA POLYMERASE LAMBDA-BASED ANTITERMINATION COMPLEX
Method: EM (single particle) / Resolution: 3.7 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ZN:
Unknown entry

Source
  • Escherichia coli (E. coli)
  • escherichia coli o157:h7 (bacteria)
  • escherichia phage lambda (virus)
  • synthetic construct (others)
KeywordsTRANSCRIPTION / TRANSCRIPTION/DNA/RNA / DNA-DEPENDENT RNA POLYMERASE / BACTERIAL TRANSCRIPTION / TERNARY ELONGATION COMPLEX / ANTITERMINATION / TRANSCRIPTION-DNA-RNA COMPLEX

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