ArticleNucleic acids research2020
Structural basis of non-canonical transcriptional regulation by the σA-bound iron-sulfur protein WhiB1 in M. tuberculosis.
Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 21 citations in OpenAlex.
- The WhiA and WhiB2 transcription factors mediate theNAR molecular medicine · 2026Article
- Cell-free genomics reveals fundamental regulatory principles of the Mycobacterium tuberculosis transcription cycle.Molecular cell · 2026Article
- Aromatic patch in whiB-like transcription factors facilitates primary sigma factor interaction in mycobacterium tuberculosis.Communications biology · 2026Article
- Iron at the crossroads of host-microbiome interactions in health and disease.Nature microbiology · 2025Review
- WhiB-like proteins: Diversity of structure, function and mechanism.Biochimica et biophysica acta. Molecular cell research · 2024Review
- Structural basis of dual activation of cell division by the actinobacterial transcription factors WhiA and WhiB.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- The essentialScience advances · 2022Article
- Photoglobin, a distinct family of non-heme binding globins, defines a potential photosensor in prokaryotic signal transduction systems.Computational and structural biotechnology journal · 2022Article
- Structural basis of transcriptional activation by the Mycobacterium tuberculosis intrinsic antibiotic-resistance transcription factor WhiB7.Molecular cell · 2021Article
- Structural insights into the functional divergence of WhiB-like proteins in Mycobacterium tuberculosis.Molecular cell · 2021Article
- Interaction of theThe Journal of biological chemistry · 2020Article
- Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
WhiB1 is a monomeric iron-sulfur cluster-containing transcription factor in the WhiB-like family that is widely distributed in actinobacteria including the notoriously persistent pathogen Mycobacterium tuberculosis (M. tuberculosis). WhiB1 plays multiple roles in regulating cell growth and responding to nitric oxide stress in M. tuberculosis, but its underlying mechanism is unclear. Here we report a 1.85 Å-resolution crystal structure of the [4Fe-4S] cluster-bound (holo-) WhiB1 in complex with the C-terminal domain of the σ70-family primary sigma factor σA of M. tuberculosis containing the conserved region 4 (σA4). Region 4 of the σ70-family primary sigma factors is commonly used by transcription factors for gene activation, and holo-WhiB1 has been proposed to activate gene expression via binding to σA4. The complex structure, however, unexpectedly reveals that the interaction between WhiB1 and σA4 is dominated by hydrophobic residues in the [4Fe-4S] cluster binding pocket, distinct from previously characterized canonical σ704-bound transcription activators. Furthermore, we show that holo-WhiB1 represses transcription by interaction with σA4in vitro and that WhiB1 must interact with σA4 to perform its essential role in supporting cell growth in vivo. Together, these results demonstrate that holo-WhiB1 regulates gene expression by a non-canonical mechanism relative to well-characterized σA4-dependent transcription activators.
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