Structural basis for transcription activation through cooperative recruitment of MntR

Haoyuan Shi, Yu Fu, Vilmante Kodyte, Amelie Andreas, Ankita J. Sachla, Keikilani Miller, Ritu Shrestha, John D. Helmann, Arthur Glasfeld and Shivani Ahuja ()
Additional contact information
Haoyuan Shi: Reed College
Yu Fu: Reed College
Vilmante Kodyte: Reed College
Amelie Andreas: Reed College
Ankita J. Sachla: Cornell University
Keikilani Miller: Reed College
Ritu Shrestha: Refeyn Inc
John D. Helmann: Cornell University
Arthur Glasfeld: Reed College
Shivani Ahuja: Reed College

Nature Communications, 2025, vol. 16, issue 1, 1-11

Abstract: Abstract Bacillus subtilis MntR is a dual regulatory protein that responds to heightened Mn2+ 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 Mn2+ 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.

Date: 2025
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-025-57412-6 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-57412-6

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-025-57412-6

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().