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TitleStructural and functional characterization of AfsR, an SARP family transcriptional activator of antibiotic biosynthesis in Streptomyces.
Journal, issue, pagesPLoS Biol, Vol. 22, Issue 3, Page e3002528, Year 2024
Publish dateMar 1, 2024
AuthorsYiqun Wang / Xu Yang / Feng Yu / Zixin Deng / Shuangjun Lin / Jianting Zheng /
PubMed AbstractStreptomyces antibiotic regulatory proteins (SARPs) are widely distributed activators of antibiotic biosynthesis. Streptomyces coelicolor AfsR is an SARP regulator with an additional nucleotide- ...Streptomyces antibiotic regulatory proteins (SARPs) are widely distributed activators of antibiotic biosynthesis. Streptomyces coelicolor AfsR is an SARP regulator with an additional nucleotide-binding oligomerization domain (NOD) and a tetratricopeptide repeat (TPR) domain. Here, we present cryo-electron microscopy (cryo-EM) structures and in vitro assays to demonstrate how the SARP domain activates transcription and how it is modulated by NOD and TPR domains. The structures of transcription initiation complexes (TICs) show that the SARP domain forms a side-by-side dimer to simultaneously engage the afs box overlapping the -35 element and the σHrdB region 4 (R4), resembling a sigma adaptation mechanism. The SARP extensively interacts with the subunits of the RNA polymerase (RNAP) core enzyme including the β-flap tip helix (FTH), the β' zinc-binding domain (ZBD), and the highly flexible C-terminal domain of the α subunit (αCTD). Transcription assays of full-length AfsR and truncated proteins reveal the inhibitory effect of NOD and TPR on SARP transcription activation, which can be eliminated by ATP binding. In vitro phosphorylation hardly affects transcription activation of AfsR, but counteracts the disinhibition of ATP binding. Overall, our results present a detailed molecular view of how AfsR serves to activate transcription.
External linksPLoS Biol / PubMed:38427710 / PubMed Central
MethodsEM (single particle)
Resolution3.35 - 5.1 Å
Structure data

EMDB-35046: Focused map on the aCTD-AfsR-DNA region of the Streptomyces coelicolor AfsR-dependent transcription activation complex
Method: EM (single particle) / Resolution: 3.77 Å

35047

8hvr

EMDB-35047, PDB-8hvr:
Cryo-EM structure of AfsR-dependent transcription activation complex with afsS promoter
Method: EM (single particle) / Resolution: 3.35 Å

EMDB-36369: Focused map on the aCTD-AfsR(T337A) region of the Streptomyces coelicolor RNAP-promoter open complex with AfsR(T337A) dimer
Method: EM (single particle) / Resolution: 5.1 Å

36370

8jke

EMDB-36370, PDB-8jke:
AfsR(T337A) transcription activation complex
Method: EM (single particle) / Resolution: 3.67 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ZN:
Unknown entry

Source
  • streptomyces coelicolor a3(2) (bacteria)
KeywordsGENE REGULATION / RNA polymerase / SARP regulator / TRANSCRIPTION / GENE REGULATION/DNA / GENE REGULATION-DNA complex

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