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-Structure paper
タイトル | Structural insights into transcription activation of the antibiotic regulatory protein, AfsR. |
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ジャーナル・号・ページ | iScience, Vol. 27, Issue 8, Page 110421, Year 2024 |
掲載日 | 2024年8月16日 |
![]() | Jing Shi / Zonghang Ye / Zhenzhen Feng / Aijia Wen / Lu Wang / Zhipeng Zhang / Liqiao Xu / Qian Song / Fulin Wang / Tianyu Liu / Shuang Wang / Yu Feng / Wei Lin / ![]() |
PubMed 要旨 | The antibiotic regulatory proteins (SARPs) are ubiquitously distributed transcription activators in and control antibiotics biosynthesis and morphological differentiation. However, the molecular ...The antibiotic regulatory proteins (SARPs) are ubiquitously distributed transcription activators in and control antibiotics biosynthesis and morphological differentiation. However, the molecular mechanism behind SARP-dependent transcription initiation remains elusive. We here solve the cryo-EM structure of an AfsR-loading RNA polymerase (RNAP)-promoter intermediate complex (AfsR-RPi) including the RNAP, a large SARP member AfsR, and its target promoter DNA that retains the upstream portion straight. The structure reveals that one dimeric N-terminal AfsR-SARP domain (AfsR-SARP) specifically engages with the same face of the AfsR-binding sites by the conserved DNA-binding domains (DBDs), replacing σR4 to bind the suboptimal -35 element, and shortens the spacer between the -10 and -35 elements. Notably, the AfsR-SARPs also recruit RNAP through extensively interacting with its conserved domains (β flap, σR4, and αCTD). Thus, these macromolecular snapshots support a general model and provide valuable clues for SARP-dependent transcription activation in . |
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手法 | EM (単粒子) |
解像度 | 3.4 Å |
構造データ | EMDB-36914, PDB-8k60: |
化合物 | ![]() ChemComp-MG: ![]() ChemComp-ZN: |
由来 |
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![]() | GENE REGULATION / transcription factor / TRANSCRIPTION-DNA complex |