ArticleThe Journal of biological chemistry2010
Domain structure of virulence-associated response regulator PhoP of Mycobacterium tuberculosis: role of the linker region in regulator-promoter interaction(s).
Article in The Journal of biological chemistry, 2010. 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
- An updated overview on the bacterial PhoP/PhoQ two-component signal transduction system.Frontiers in cellular and infection microbiology · 2025Review
- Article
- Dual functioning by the PhoR sensor is a key determinant to Mycobacterium tuberculosis virulence.PLoS genetics · 2023Article
- The pathogenic mechanism of Mycobacterium tuberculosis: implication for new drug development.Molecular biomedicine · 2022Review
- 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
- A Low-Prevalence Single-Nucleotide Polymorphism in the Sensor Kinase PhoR inFrontiers in microbiology · 2021Article
- Metabolic Switching ofJournal of bacteriology · 2020Article
- Cloning, Expression and Purification of Espc, Espb and Espc/Espb Proteins ofReports of biochemistry & molecular biology · 2020Article
- Functioning of Mycobacterial Heat Shock Repressors Requires the Master Virulence Regulator PhoP.Journal of bacteriology · 2019Article
- Solution NMR Studies of Mycobacterium tuberculosis Proteins for Antibiotic Target Discovery.Molecules (Basel, Switzerland) · 2017Review
- Rapid addition of unlabeled silent solubility tags to proteins using a new substrate-fused sortase reagent.Journal of biomolecular NMR · 2016Article
- Solution structure of the PhoP DNA-binding domain from Mycobacterium tuberculosis.Journal of biomolecular NMR · 2015Article
- 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
- Phosphorylation of PhoP protein plays direct regulatory role in lipid biosynthesis of Mycobacterium tuberculosis.The Journal of biological chemistry · 2011Article
- Structure of the response regulator PhoP from Mycobacterium tuberculosis reveals a dimer through the receiver domain.Biochemistry · 2011Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The PhoP and PhoR proteins from Mycobacterium tuberculosis form a highly specific two-component system that controls expression of genes involved in complex lipid biosynthesis and regulation of unknown virulence determinants. The several functions of PhoP are apportioned between a C-terminal effector domain (PhoPC) and an N-terminal receiver domain (PhoPN), phosphorylation of which regulates activation of the effector domain. Here we show that PhoPN, on its own, demonstrates PhoR-dependent phosphorylation. PhoPC, the truncated variant bearing the DNA binding domain, binds in vitro to the target site with affinity similar to that of the full-length protein. To complement the finding that residues spanning Met(1) to Arg(138) of PhoP constitute the minimal functional PhoPN, we identified Arg(150) as the first residue of the distal PhoPC domain capable of DNA binding on its own, thereby identifying an interdomain linker. However, coupling of two functional domains together in a single polypeptide chain is essential for phosphorylation-coupled DNA binding by PhoP. We discuss consequences of tethering of two domains on DNA binding and demonstrate that linker length and not individual residues of the newly identified linker plays a critical role in regulating interdomain interactions. Together, these results have implications for the molecular mechanism of transmission of conformation change associated with phosphorylation of PhoP that results in the altered DNA recognition by the C-terminal domain.
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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.