ArticleJournal of bacteriology2009
Mycobacterium tuberculosis PhoP recognizes two adjacent direct-repeat sequences to form head-to-head dimers.
Article in Journal of bacteriology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 38 citations in OpenAlex.
- Transcriptional control of asparagine utilization regulates mycobacterial pH-driven adaptation at the host-pathogen crossroads.The Journal of biological chemistry · 2026Article
- Structural insights into transcription regulation of the global OmpR/PhoB family regulator PhoP from Mycobacterium tuberculosis.Nature communications · 2025Article
- Clinically relevant mutations in the PhoR sensor kinase of host-adaptedMicrobiology spectrum · 2023Article
- Dual functioning by the PhoR sensor is a key determinant to Mycobacterium tuberculosis virulence.PLoS genetics · 2023Article
- Convergence of two global regulators to coordinate expression of essential virulence determinants ofeLife · 2022Article
- Molecular Connectivity between Extracytoplasmic Sigma Factors and PhoP Accounts for Coupled Mycobacterial Stress Response.Journal of bacteriology · 2022Article
- Deletion of the Response Regulator PhoP Accelerates the Formation of Aerial Mycelium and Spores inFrontiers in microbiology · 2022Article
- Metabolic Switching ofJournal of bacteriology · 2020Article
- Functioning of Mycobacterial Heat Shock Repressors Requires the Master Virulence Regulator PhoP.Journal of bacteriology · 2019Article
- The wing of the ToxR winged helix-turn-helix domain is required for DNA binding and activation of toxT and ompU.PloS one · 2019Article
- PhoPR Positively RegulatesJournal of bacteriology · 2018Article
- EspR-dependent ESAT-6 Protein Secretion of Mycobacterium tuberculosis Requires the Presence of Virulence Regulator PhoP.The Journal of biological chemistry · 2016Article
- Review
- DNA consensus sequence motif for binding response regulator PhoP, a virulence regulator of Mycobacterium tuberculosis.Biochemistry · 2014Article
- Unique N-terminal arm of Mycobacterium tuberculosis PhoP protein plays an unusual role in its regulatory function.The Journal of biological chemistry · 2013Article
- Interactions of the CpxA sensor kinase and cognate CpxR response regulator from Yersinia pseudotuberculosis.BMC research notes · 2012Article
- Identification of DNA binding motifs of the Mycobacterium tuberculosis PhoP/PhoR two-component signal transduction system.PloS one · 2012Article
- Phosphorylation of PhoP protein plays direct regulatory role in lipid biosynthesis of Mycobacterium tuberculosis.The Journal of biological chemistry · 2011Article
- Adaptation to environmental stimuli within the host: two-component signal transduction systems of Mycobacterium tuberculosis.Microbiology and molecular biology reviews : MMBR · 2011Review
- Domain structure of virulence-associated response regulator PhoP of Mycobacterium tuberculosis: role of the linker region in regulator-promoter interaction(s).The Journal of biological chemistry · 2010Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mycobacterium tuberculosis PhoP of the PhoP-PhoR two-component signaling system orchestrates a complex transcription program and is essential for the growth and virulence of the tubercle bacillus. PhoP comprises a phosphorylation domain at the amino-terminal half and a DNA-binding domain in the carboxy-terminal half of the protein. We show here that the protein recognizes a 23-bp sequence of the phoP upstream region comprising two adjacent direct repeat motifs believed to promote transcription regulation. DNA binding, which involves the recruitment of two monomeric PhoP molecules, was dependent on conserved adenines of the repeat sequences and the orientation of the repeat motifs relative to each other. Although response regulators such as PhoB and FixJ dimerize upon phosphorylation, we demonstrate here that PhoP dimerization can also be stimulated by DNA binding. Using the established asymmetric tandem binding model by members of the OmpR/PhoB protein family as a guide, we set out to examine intermolecular interactions between PhoP dimers by protein cross-linking. Our results are consistent with a model in which two PhoP protomers bind the duplex DNA with a symmetric head-to-head orientation to project their N termini toward one another, arguing against previously proposed head-to-tail tandem dimer formation for members of the OmpR/PhoB protein subfamily.
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Registered trials
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.