ArticleJournal of bacteriology2014
HupB, a nucleoid-associated protein of Mycobacterium tuberculosis, is modified by serine/threonine protein kinases in vivo.
Article in Journal of bacteriology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 74 citations in OpenAlex.
- Protein kinase F regulates the virulence ofInfection and immunity · 2026Article
- Nucleoid-associated protein HU constrains transcription elongation to influence cellular functions, virulence, and drug tolerance in Mycobacterium tuberculosis.Nucleic acids research · 2026Article
- Molecular Kaleidoscope of Nucleoid-Associated Proteins Regulatory Network and Chromosome Architecture in Mycobacterium Tuberculosis.Current microbiology · 2026Review
- PTM-associated condensation of homopolymeric (poly A) RNA by MDP1.Biophysics and physicobiology · 2026Article
- Structural Studies on the M. tuberculosis Nucleoid-associated-Protein, NapA, Indicates DNA Bridging Mechanism.Journal of molecular biology · 2025Article
- Protein kinase F regulates the virulence ofbioRxiv : the preprint server for biology · 2025Article
- Genomic and Computational Analysis Unveils Bacteriocin Based Therapeutics against Clinical Mastitis Pathogens in Dairy Cows.Probiotics and antimicrobial proteins · 2025Article
- Intercellular mosaic methylation in fast-growingNAR molecular medicine · 2024Article
- Review
- Stress-induced nucleoid remodeling in Deinococcus radiodurans is associated with major changes in Heat Unstable (HU) protein dynamics.Nucleic acids research · 2024Article
- Shedding Light on Bacterial Chromosome Structure: Exploring the Significance of 3C-Based Approaches.Methods in molecular biology (Clifton, N.J.) · 2024Review
- The Mycobacterium tuberculosis methyltransferase Rv2067c manipulates host epigenetic programming to promote its own survival.Nature communications · 2023Article
- Development of a new cellular immunological detection method for tuberculosis based on HupB protein induced IL-6 release test.Frontiers in microbiology · 2023Article
- Mycobacterial IHF is a highly dynamic nucleoid-associated protein that assists HupB in organizing chromatin.Frontiers in microbiology · 2023Article
- Arginine 58 is indispensable for proper function of theVirulence · 2022Article
- Types and functions of heterogeneity in mycobacteria.Nature reviews. Microbiology · 2022Review
- Role of serine/threonine protein phosphatase PrpN in the life cycle of Bacillus anthracis.PLoS pathogens · 2022Article
- Small Prokaryotic DNA-Binding Proteins Protect Genome Integrity throughout the Life Cycle.International journal of molecular sciences · 2022Review
- Phosphorylation and acetylation of mitochondrial transcription factor A promote transcription processivity without compromising initiation or DNA compaction.The Journal of biological chemistry · 2022Article
- HupB, a nucleoid-associated protein, is critical for survival ofFrontiers in microbiology · 2022Article
Corrections and comments
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Authors and funding
9 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
HU, a widely conserved bacterial histone-like protein, regulates many genes, including those involved in stress response and virulence. Whereas ample data are available on HU-DNA communication, the knowledge on how HU perceives a signal and transmit it to DNA remains limited. In this study, we identify HupB, the HU homolog of the human pathogen Mycobacterium tuberculosis, as a component of serine/threonine protein kinase (STPK) signaling. HupB is extracted in its native state from the exponentially growing cells of M. tuberculosis H37Ra and is shown to be phosphorylated on both serine and threonine residues. The STPKs capable of modifying HupB are determined in vitro and the residues modified by the STPKs are identified for both in vivo and the in vitro proteins through mass spectrometry. Of the identified phosphosites, Thr(65) and Thr(74) in the DNA-embracing β-strand of the N-terminal domain of HupB (N-HupB) are shown to be crucial for its interaction with DNA. In addition, Arg(55) is also identified as an important residue for N-HupB-DNA interaction. N-HupB is shown to have a diminished interaction with DNA after phosphorylation. Furthermore, hupB is shown to be maximally expressed during the stationary phase in M. tuberculosis H37Ra, while HupB kinases were found to be constitutively expressed (PknE and PknF) or most abundant during the exponential phase (PknB). In conclusion, HupB, a DNA-binding protein, with an ability to modulate chromatin structure is proposed to work in a growth-phase-dependent manner through its phosphorylation carried out by the mycobacterial STPKs.
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