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Title | Structural basis of λCII-dependent transcription activation. |
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Journal, issue, pages | Structure, Vol. 31, Issue 8, Page 968-974.e3, Year 2023 |
Publish date | Aug 3, 2023 |
Authors | Minxing Zhao / Bo Gao / Aijia Wen / Yu Feng / Yuan-Qiang Lu / |
PubMed Abstract | The CII protein of bacteriophage λ activates transcription from the phage promoters P, P, and P by binding to two direct repeats that straddle the promoter -35 element. Although genetic, ...The CII protein of bacteriophage λ activates transcription from the phage promoters P, P, and P by binding to two direct repeats that straddle the promoter -35 element. Although genetic, biochemical, and structural studies have elucidated many aspects of λCII-mediated transcription activation, no precise structure of the transcription machinery in the process is available. Here, we report a 3.1-Å cryo-electron microscopy (cryo-EM) structure of an intact λCII-dependent transcription activation complex (TAC-λCII), which comprises λCII, E. coli RNAP-σ holoenzyme, and the phage promoter P. The structure reveals the interactions between λCII and the direct repeats responsible for promoter specificity and the interactions between λCII and RNAP α subunit C-terminal domain responsible for transcription activation. We also determined a 3.4-Å cryo-EM structure of an RNAP-promoter open complex (RPo-P) from the same dataset. Structural comparison between TAC-λCII and RPo-P provides new insights into λCII-dependent transcription activation. |
External links | Structure / PubMed:37269829 |
Methods | EM (single particle) |
Resolution | 3.1 - 3.4 Å |
Structure data | EMDB-35438, PDB-8igr: EMDB-35439, PDB-8igs: |
Chemicals | ChemComp-MG: ChemComp-ZN: |
Source |
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Keywords | TRANSCRIPTION / RNA polymerase / transcription activation / bacteriophage / CII |