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Structure paper

TitleStructural insights into the transcription activation mechanism of the global regulator GlnR from actinobacteria.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 120, Issue 22, Page e2300282120, Year 2023
Publish dateMay 30, 2023
AuthorsJing Shi / Zhenzhen Feng / Juncao Xu / Fangfang Li / Yuqiong Zhang / Aijia Wen / Fulin Wang / Qian Song / Lu Wang / Hong Cui / Shujuan Tong / Peiying Chen / Yejin Zhu / Guoping Zhao / Shuang Wang / Yu Feng / Wei Lin /
PubMed AbstractIn actinobacteria, an OmpR/PhoB subfamily protein called GlnR acts as an orphan response regulator and globally coordinates the expression of genes responsible for nitrogen, carbon, and phosphate ...In actinobacteria, an OmpR/PhoB subfamily protein called GlnR acts as an orphan response regulator and globally coordinates the expression of genes responsible for nitrogen, carbon, and phosphate metabolism in actinobacteria. Although many researchers have attempted to elucidate the mechanisms of GlnR-dependent transcription activation, progress is impeded by lacking of an overall structure of GlnR-dependent transcription activation complex (GlnR-TAC). Here, we report a co-crystal structure of the C-terminal DNA-binding domain of GlnR (GlnR_DBD) in complex with its regulatory -element DNA and a cryo-EM structure of GlnR-TAC which comprises RNA polymerase, GlnR, and a promoter containing four well-characterized conserved GlnR binding sites. These structures illustrate how four GlnR protomers coordinate to engage promoter DNA in a head-to-tail manner, with four N-terminal receiver domains of GlnR (GlnR-RECs) bridging GlnR_DBDs and the RNAP core enzyme. Structural analysis also unravels that GlnR-TAC is stabilized by complex protein-protein interactions between GlnR and the conserved β flap, σR4, αCTD, and αNTD domains of RNAP, which are further confirmed by our biochemical assays. Taken together, these results reveal a global transcription activation mechanism for the master regulator GlnR and other OmpR/PhoB subfamily proteins and present a unique mode of bacterial transcription regulation.
External linksProc Natl Acad Sci U S A / PubMed:37216560 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.95 - 3.66 Å
Structure data

34816

8hih

EMDB-34816, PDB-8hih:
Cryo-EM structure of Mycobacterium tuberculosis transcription initiation complex with transcription factor GlnR
Method: EM (single particle) / Resolution: 3.66 Å

PDB-8hml:
Co-crystal structure of the C terminal DNA binding domain of Saccharopolyspora erythraea GlnR in complex with its conserved promoter DNA in 2.95 Angstrom resolution
Method: X-RAY DIFFRACTION / Resolution: 2.95 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

Source
  • mycobacterium tuberculosis (bacteria)
  • mycobacterium tuberculosis h37rv (bacteria)
  • saccharopolyspora erythraea nrrl 2338 (bacteria)
KeywordsTRANSCRIPTION/DNA / transcription factor / TRANSCRIPTION-DNA complex / TRANSFERASE/DNA / methylenetetrahydrofolate reductase / TRANSFERASE-DNA COMPLEX

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