ArticleNature communications2019
Structure and functional implications of WYL domain-containing bacterial DNA damage response regulator PafBC.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 37 citations in OpenAlex.
- Transcription activation mechanism of a noncanonical DNA damage response pathway by the WYL-activator, DriD.Science advances · 2026Article
- A WYL transcriptional regulator activates the DNA damage response pathway in Acinetobacter species.Nucleic acids research · 2026Article
- Stress genomics of the toxigenic cyanobacteria: environmental and biotechnological perspectives.World journal of microbiology & biotechnology · 2025Review
- DdiA, an XRE family transcriptional regulator, is a co-regulator of the DNA damage response inJournal of bacteriology · 2025Article
- Allosteric activation mechanism of DriD, a WYL-domain containing transcription regulator.Communications biology · 2025Article
- A WYL domain transcription factor regulates Lactiplantibacillus plantarum intestinal colonization via perceiving c-di-GMP.Nature communications · 2025Article
- Single-stranded DNA binding to the transcription factor PafBC triggers the mycobacterial DNA damage response.Science advances · 2025Article
- Bacterial WYL domain transcriptional repressors sense single-stranded DNA to control gene expression.Nucleic acids research · 2024Article
- RIP-seq reveals RNAs that interact with RNA polymerase and primary sigma factors in bacteria.Nucleic acids research · 2024Article
- Structure of the WYL-domain containing transcription activator, DriD, in complex with ssDNA effector and DNA target site.Nucleic acids research · 2024Article
- Novel WYL domain-containing transcriptional activator acts in response to genotoxic stress in rapidly growing mycobacteria.Communications biology · 2023Article
- Electrostatic interactions guide substrate recognition of the prokaryotic ubiquitin-like protein ligase PafA.Nature communications · 2023Article
- SOS-independent bacterial DNA damage responses: diverse mechanisms, unifying function.Current opinion in microbiology · 2023Review
- Structural Studies of Pif1 Helicases from Thermophilic Bacteria.Microorganisms · 2023Article
- A widespread family of WYL-domain transcriptional regulators co-localizes with diverse phage defence systems and islands.Nucleic acids research · 2022Article
- Control of bacterial immune signaling by a WYL domain transcription factor.Nucleic acids research · 2022Article
- Identification and characterization of the WYL BrxR protein and its gene as separable regulatory elements of a BREX phage restriction system.Nucleic acids research · 2022Article
- ssDNA is an allosteric regulator of theGenes & development · 2022Article
- Division of labor between SOS and PafBC in mycobacterial DNA repair and mutagenesis.Nucleic acids research · 2021Article
- Transcriptional control of mycobacterial DNA damage response by sigma adaptation.Science advances · 2021Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In mycobacteria, transcriptional activator PafBC is responsible for upregulating the majority of genes induced by DNA damage. Understanding the mechanism of PafBC activation is impeded by a lack of structural information on this transcription factor that contains a widespread, but poorly understood WYL domain frequently encountered in bacterial transcription factors. Here, we determine the crystal structure of Arthrobacter aurescens PafBC. The protein consists of two modules, each harboring an N-terminal helix-turn-helix DNA-binding domain followed by a central WYL and a C-terminal extension (WCX) domain. The WYL domains exhibit Sm-folds, while the WCX domains adopt ferredoxin-like folds, both characteristic for RNA-binding proteins. Our results suggest a mechanism of regulation in which WYL domain-containing transcription factors may be activated by binding RNA or other nucleic acid molecules. Using an in vivo mutational screen in Mycobacterium smegmatis, we identify potential co-activator binding sites on PafBC.
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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.