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TitleStructural basis for transcription activation through cooperative recruitment of MntR.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 2204, Year 2025
Publish dateMar 5, 2025
AuthorsHaoyuan Shi / Yu Fu / Vilmante Kodyte / Amelie Andreas / Ankita J Sachla / Keikilani Miller / Ritu Shrestha / John D Helmann / Arthur Glasfeld / Shivani Ahuja /
PubMed AbstractBacillus subtilis MntR is a dual regulatory protein that responds to heightened Mn availability in the cell by both repressing the expression of uptake transporters and activating the expression of ...Bacillus subtilis MntR is a dual regulatory protein that responds to heightened Mn availability in the cell by both repressing the expression of uptake transporters and activating the expression of efflux proteins. Recent work indicates that, in its role as an activator, MntR binds several sites upstream of the genes encoding Mn exporters, leading to a cooperative response to manganese. Here, we use cryo-EM to explore the molecular basis of gene activation by MntR and report a structure of four MntR dimers bound to four 18-base pair sites across an 84-base pair regulatory region of the mneP promoter. Our structures, along with solution studies including mass photometry and in vivo transcription assays, reveal that MntR dimers employ polar and non-polar contacts to bind cooperatively to an array of low-affinity DNA-binding sites. These results reveal the molecular basis for cooperativity in the activation of manganese efflux.
External linksNat Commun / PubMed:40044701 / PubMed Central
MethodsEM (single particle)
Resolution3.09 - 4.17 Å
Structure data

45181

9c4c

EMDB-45181: The structure of two MntR dimers bound to the native mnep promoter sequence.
PDB-9c4c: The structure of two MntR dimers bound to the native mnep promoter sequence
Method: EM (single particle) / Resolution: 3.09 Å

45182

9c4d

EMDB-45182: The structure of 4 MntR homodimers bound to the promoter sequence of mnep.
PDB-9c4d: The structure of 4 MntR homodimers bound to the promoter sequence of mnep
Method: EM (single particle) / Resolution: 4.17 Å

Chemicals

ChemComp-MN:
Unknown entry

Source
  • bacillus subtilis (bacteria)
KeywordsGENE REGULATION / Manganese / metal ion homeostasis / transcription regulation / transcription activation / cooperative binding / DNA binding

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