Structural basis of AlpA-dependent transcription antitermination

التفاصيل البيبلوغرافية
العنوان: Structural basis of AlpA-dependent transcription antitermination
المؤلفون: Aijia Wen, Minxing Zhao, Sha Jin, Yuan-Qiang Lu, Yu Feng
المصدر: Nucleic Acids Research. 50:8321-8330
بيانات النشر: Oxford University Press (OUP), 2022.
سنة النشر: 2022
مصطلحات موضوعية: Bacterial Proteins, Transcription, Genetic, Protein Conformation, Cryoelectron Microscopy, Pseudomonas aeruginosa, Genetics, RNA, RNA-Binding Proteins, DNA-Directed RNA Polymerases, Promoter Regions, Genetic
الوصف: AlpA positively regulates a programmed cell death pathway linked to the virulence of Pseudomonas aeruginosa by recognizing an AlpA binding element within the promoter, then binding RNA polymerase directly and allowing it to bypass an intrinsic terminator positioned downstream. Here, we report the single-particle cryo-electron microscopy structures of both an AlpA-loading complex and an AlpA-loaded complex. These structures indicate that the C-terminal helix-turn-helix motif of AlpA binds to the AlpA binding element and that the N-terminal segment of AlpA forms a narrow ring inside the RNA exit channel. AlpA was also revealed to render RNAP resistant to termination signals by prohibiting RNA hairpin formation in the RNA exit channel. Structural analysis predicted that AlpA, 21Q, λQ and 82Q share the same mechanism of transcription antitermination.
تدمد: 1362-4962
0305-1048
DOI: 10.1093/nar/gkac608
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::352839f3f537e84b8ad5bcfe3a470500
https://doi.org/10.1093/nar/gkac608
Rights: OPEN
رقم الانضمام: edsair.doi.dedup.....352839f3f537e84b8ad5bcfe3a470500
قاعدة البيانات: OpenAIRE
الوصف
تدمد:13624962
03051048
DOI:10.1093/nar/gkac608