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HupB, a Nucleoid-Associated Protein of Mycobacterium tuberculosis, Is Modified by Serine/Threonine Protein Kinases In Vivo
- Source :
- Journal of Bacteriology. 196:2646-2657
- Publication Year :
- 2014
- Publisher :
- American Society for Microbiology, 2014.
-
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 H 37 Ra 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 H 37 Ra, 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.
- Subjects :
- DNA, Bacterial
Molecular Sequence Data
Serine threonine protein kinase
Protein Serine-Threonine Kinases
Biology
Microbiology
DNA-binding protein
Gene Expression Regulation, Enzymologic
Histones
Serine
Bacterial Proteins
Humans
Amino Acid Sequence
Cloning, Molecular
Phosphorylation
Protein kinase A
Molecular Biology
Microbiology & Cell Biology
Protein-Serine-Threonine Kinases
Kinase
Gene Expression Regulation, Bacterial
Mycobacterium tuberculosis
Articles
Chromatin
Biochemistry
Protein Binding
Subjects
Details
- ISSN :
- 10985530 and 00219193
- Volume :
- 196
- Database :
- OpenAIRE
- Journal :
- Journal of Bacteriology
- Accession number :
- edsair.doi.dedup.....fa9c0b0ad6188662ef15089230e65ddd
- Full Text :
- https://doi.org/10.1128/jb.01625-14