Structural insights into the mycobacteria transcription initiation complex from analysis of X-ray crystal structures [electronic resource]

• Ngôn ngữ: eng
• Ký hiệu phân loại: 572.6 Proteins
• Thông tin xuất bản: Washington, D.C. : Oak Ridge, Tenn. : United States. Dept. of Energy. Office of Science ; Distributed by the Office of Scientific and Technical Information, U.S. Dept. of Energy, 2017
• Mô tả vật lý: Size: Article No. 16072 : , digital, PDF file.
• Bộ sưu tập: Metadata
• ID: 260418
• Chủ đề: 1. 60 applied life sciences

Tóm tắt

 The mycobacteria RNA polymerase (RNAP) is a target for antimicrobials against tuberculosis, motivating structure/function studies. Here we report a 3.2 �-resolution crystal structure of a Mycobacterium smegmatis (Msm) open promoter complex (RPo), along with structural analysis of the Msm RPo and a previously reported 2.76 �-resolution crystal structure of an Msm transcription initiation complex with a promoter DNA fragment. We observe the interaction of the Msm RNAP ?-subunit C-terminal domain (?CTD) with DNA, and we provide evidence that the a CTD may play a role in Mtb transcription regulation. Here, our results reveal the structure of an Actinobacteria-unique insert of the RNAP ?' subunit. Finally, our analysis reveals the disposition of the N-terminal segment of Msm ?<
 sup>
 A<
 /sup>
 , which may comprise an intrinsically disordered protein domain unique to mycobacteria. The clade-specific features of the mycobacteria RNAP provide clues to the profound instability of mycobacteria RPo compared with E. coli.