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-Structure paper
Title | Structural basis of Q-dependent antitermination. |
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Journal, issue, pages | Proc Natl Acad Sci U S A, Vol. 116, Issue 37, Page 18384-18390, Year 2019 |
Publish date | Sep 10, 2019 |
Authors | Zhou Yin / Jason T Kaelber / Richard H Ebright / |
PubMed Abstract | Lambdoid bacteriophage Q protein mediates the switch from middle to late bacteriophage gene expression by enabling RNA polymerase (RNAP) to read through transcription terminators preceding ...Lambdoid bacteriophage Q protein mediates the switch from middle to late bacteriophage gene expression by enabling RNA polymerase (RNAP) to read through transcription terminators preceding bacteriophage late genes. Q loads onto RNAP engaged in promoter-proximal pausing at a Q binding element (QBE) and adjacent sigma-dependent pause element (SDPE) to yield a Q-loading complex, and Q subsequently translocates with RNAP as a pausing-deficient, termination-deficient Q-loaded complex. Here, we report high-resolution structures of 4 states on the pathway of antitermination by Q from bacteriophage 21 (Q21): Q21, the Q21-QBE complex, the Q21-loading complex, and the Q21-loaded complex. The results show that Q21 forms a torus, a "nozzle," that narrows and extends the RNAP RNA-exit channel, extruding topologically linked single-stranded RNA and preventing the formation of pause and terminator hairpins. |
External links | Proc Natl Acad Sci U S A / PubMed:31455742 / PubMed Central |
Methods | EM (single particle) / X-ray diffraction |
Resolution | 1.942 - 3.8 Å |
Structure data | EMDB-20233, PDB-6p18: EMDB-20234, PDB-6p19: PDB-6p1a: PDB-6p1b: PDB-6p1c: |
Chemicals | ChemComp-ZN: ChemComp-MG: ChemComp-EDO: ChemComp-CL: ChemComp-HOH: |
Source |
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Keywords | GENE REGULATION / RNA polymerase / DNA Binding / transcription / Q-dependent antitermination / Q antiterminator factor / Q antitermination factor |