ArticleThe Journal of biological chemistry2013
WhiB7, an Fe-S-dependent transcription factor that activates species-specific repertoires of drug resistance determinants in actinobacteria.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 57 citations in OpenAlex.
- Tobramycin enhancesProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Activation of the antibiotic resistance factor WhiB7 can stimulate aggregate biofilm formation in stationary phaseJournal of bacteriology · 2026Article
- Regulation of Dormancy-Associated GenesACS omega · 2026Article
- Prodrug florfenicol amine is activated by intrinsic resistance to target Mycobacterium abscessus.Nature microbiology · 2025Article
- WhiB-like proteins: Diversity of structure, function and mechanism.Biochimica et biophysica acta. Molecular cell research · 2024Review
- Beyond antibiotic resistance: The whiB7 transcription factor coordinates an adaptive response to alanine starvation in mycobacteria.Cell chemical biology · 2024Article
- Hierarchy and interconnected networks in the WhiB7 mediated transcriptional response to antibiotic stress in Mycobacterium abscessus.PLoS genetics · 2023Article
- Analysis of whiB7 in Mycobacterium tuberculosis reveals novel AT-hook deletion mutations.Scientific reports · 2023Article
- Beyond antibiotic resistance: thebioRxiv : the preprint server for biology · 2023Article
- Genome-wide association studies of global Mycobacterium tuberculosis resistance to 13 antimicrobials in 10,228 genomes identify new resistance mechanisms.PLoS biology · 2022Article
- An In Vivo Model of SeparateInternational journal of molecular sciences · 2022Article
- Transcriptional regulation and drug resistance inFrontiers in cellular and infection microbiology · 2022Review
- The Iron Response ofFrontiers in cellular and infection microbiology · 2022Review
- Multiform antimicrobial resistance from a metabolic mutation.Science advances · 2021Article
- Structural insights into the functional divergence of WhiB-like proteins in Mycobacterium tuberculosis.Molecular cell · 2021Article
- Increased whiB7 expression and antibiotic resistance in Mycobacterium chelonae carrying two prophages.BMC microbiology · 2021Article
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- Extremely Low Hit Rate in a Diverse Chemical Drug Screen Targeting Mycobacterium abscessus.Antimicrobial agents and chemotherapy · 2019Article
- The actinobacterial WhiB-like (Wbl) family of transcription factors.Molecular microbiology · 2018Review
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Authors and funding
11 authors at 4 institutions in 4 countries.
Funding
Abstract
WhiB-like (Wbl) proteins are well known for their diverse roles in actinobacterial morphogenesis, cell division, virulence, primary and secondary metabolism, and intrinsic antibiotic resistance. Gene disruption experiments showed that three different Actinobacteria (Mycobacterium smegmatis, Streptomyces lividans, and Rhodococcus jostii) each exhibited a different whiB7-dependent resistance profile. Heterologous expression of whiB7 genes showed these resistance profiles reflected the host's repertoire of endogenous whiB7-dependent genes. Transcriptional activation of two resistance genes in the whiB7 regulon, tap (a multidrug transporter) and erm(37) (a ribosomal methyltransferase), required interaction of WhiB7 with their promoters. Furthermore, heterologous expression of tap genes isolated from Mycobacterium species demonstrated that divergencies in drug specificity of homologous structural proteins contribute to the variation of WhiB7-dependent drug resistance. WhiB7 has a specific tryptophan/glycine-rich region and four conserved cysteine residues; it also has a peptide sequence (AT-hook) at its C terminus that binds AT-rich DNA sequence motifs upstream of the promoters it activates. Targeted mutagenesis showed that these motifs were required to provide antibiotic resistance in vivo. Anaerobically purified WhiB7 from S. lividans was dimeric and contained 2.1 ± 0.3 and 2.2 ± 0.3 mol of iron and sulfur, respectively, per protomer (consistent with the presence of a 2Fe-2S cluster). However, the properties of the dimer's absorption spectrum were most consistent with the presence of an oxygen-labile 4Fe-4S cluster, suggesting 50% occupancy. These data provide the first insights into WhiB7 iron-sulfur clusters as they exist in vivo, a major unresolved issue in studies of Wbl proteins.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.