We use cookies to improve your experience. By continuing to browse this site, you accept our cookie policy.×
Skip main navigation
Aging Health
Bioelectronics in Medicine
Biomarkers in Medicine
Breast Cancer Management
CNS Oncology
Colorectal Cancer
Concussion
Epigenomics
Future Cardiology
Future Medicine AI
Future Microbiology
Future Neurology
Future Oncology
Future Rare Diseases
Future Virology
Hepatic Oncology
HIV Therapy
Immunotherapy
International Journal of Endocrine Oncology
International Journal of Hematologic Oncology
Journal of 3D Printing in Medicine
Lung Cancer Management
Melanoma Management
Nanomedicine
Neurodegenerative Disease Management
Pain Management
Pediatric Health
Personalized Medicine
Pharmacogenomics
Regenerative Medicine

Challenges in elucidating bacteria–host epigenetic dynamics

    Valakunja Nagaraja

    *Author for correspondence: Tel.: +91 80 2360 0668;

    E-mail Address: vraj@iisc.ac.in

    Department of Microbiology & Cell Biology, Indian Institute of Science, Bangalore, 560012, India

    Jawaharlal Nehru Centre for Advanced Scientific Research, Bangalore, 560064, India

    &
    Prakruti R Singh

    Department of Microbiology & Cell Biology, Indian Institute of Science, Bangalore, 560012, India

    Published Online:https://doi.org/10.2217/epi-2021-0357
    Free first page

    Papers of special note have been highlighted as: • of interest; •• of considerable interest

    References

    • 1. Becker PB, Workman JL. Nucleosome remodeling and epigenetics. Cold Spring Harb. Perspect. Biol. 5(9), 1–19 (2013).
    • 2. Allis CD, Jenuwein T. The molecular hallmarks of epigenetic control. Nat. Rev. Genet. 17(8), 487–500 (2016).
    • 3. Murn J, Shi Y. The winding path of protein methylation research: milestones and new frontiers. Nat. Rev. Mol. Cell Biol. 18(8), 517–527 (2017).
    • 4. Dillon SC, Dorman CJ. Bacterial nucleoid-associated proteins, nucleoid structure and gene expression. Nat. Rev. Microbiol. 8, 185 (2010). • An authoritative overview describing the diverse function of nucleoid-associated proteins (NAPs) in shaping the bacterial nucleoid.
    • 5. Hu L, Kong W, Yang D, Han Q, Guo L, Shi Y. Threonine phosphorylation fine-tunes the regulatory activity of histone-like nucleoid structuring protein in Salmonella transcription. Front. Microbiol. 10, 1515 (2019).
    • 6. Carabetta VJ, Greco TM, Cristea IM, Dubnau D. YfmK is an Nε-lysine acetyltransferase that directly acetylates the histone-like protein HBsu in Bacillus subtilis. Proc. Natl Acad. Sci. USA 116(9), 3752–3757 (2019).
    • 7. Dilweg IW, Dame RT. Post-translational modification of nucleoidassociated proteins: an extra layer of functional modulation in bacteria? Biochem. Soc. Trans. 46(5), 1381–1392 (2018).
    • 8. Kapopoulou A, Lew JM, Cole ST. The MycoBrowser portal: a comprehensive and manually annotated resource for mycobacterial genomes. Tuberculosis 91(1), 8–13 (2011).
    • 9. Hentchel KL, Escalante-Semerena JC. Acylation of biomolecules in Prokaryotes: a widespread strategy for the control of biological function and metabolic stress. Microbiol. Mol. Biol. Rev. 79(3), 321–346 (2015).
    • 10. Bhowmick T, Ghosh S, Dixit K et al. Targeting mycobacterium tuberculosis nucleoid-associated protein HU with structure-based inhibitors. Nat. Commun. 5(1), 4124 (2014). •• First example of bacterial NAP targeted by small-molecule inhibitors employing structure-based drug design. The inhibitors of Mycobacterium tuberculosis (Mtb) HU alter nucleoid dynamics impacting gene expression and killing Mtb.
    • 11. Ghosh S, Padmanabhan B, Anand C, Nagaraja V. Lysine acetylation of the Mycobacterium tuberculosis HU protein modulates its DNA binding and genome organization. Mol. Microbiol. 100(4), 577–588 (2016).
    • 12. Anand C, Santoshi M, Singh PR, Nagaraja V. Rv0802c is an acyltransferase that succinylates and acetylates Mycobacterium tuberculosis nucleoid-associated protein HU. Microbiology 167(7), 001058 (2021).
    • 13. Kim KH, An DR, Song J et al. Mycobacterium tuberculosis Eis protein initiates suppression of host immune responses by acetylation of DUSP16/MKP-7. Proc. Natl Acad. Sci. USA 109(20), 7729–7734 (2012). • Mtb acetyltransferase EIS inhibits autophagy and phagosome maturation in infected macrophages by acetylating DUSP16/MKP-7 and supresses host immune responses for intracellular survival.
    • 14. Hamon MA, Cossart P. Histone modifications and chromatin remodeling during bacterial infections. Cell Host Microbe 4(2), 100–109 (2008). •• This review illustrates a number of strategies employed by various bacterial pathogens in altering the host chromatin.
    • 15. Cabezas-Cruz A, Alberdi P, Ayllón N et al. Anaplasma phagocytophilum increases the levels of histone modifying enzymes to inhibit cell apoptosis and facilitate pathogen infection in the tick vector Ixodes scapularis. Epigenetics 11(4), 303–319 (2016).
    • 16. Silmon de Monerri NC, Kim K. Pathogens hijack the epigenome: a new twist on host-pathogen interactions. Am. J. Pathol. 184(4), 897–911 (2014). • Highlights the long-lasting epigenetic changes induced by pathogens upon infection in host and non-host cells.
    • 17. Rolando M, Sanulli S, Rusniok C et al. Legionella pneumophila effector RomA uniquely modifies host chromatin to repress gene expression and promote intracellular bacterial replication. Cell Host Microbe 13(4), 395–405 (2013). •• A secretory methyltransferase of L. pneumophila enters the host nucleus and uniquely adds a repressive mark by trimethylating K14 of histone H3. The addition of the mark alters the host gene expression giving survival advantage to the bacteria.
    • 18. Yaseen I, Kaur P, Nandicoori VK, Khosla S. Mycobacteria modulate host epigenetic machinery by Rv1988 methylation of a non-tail arginine of histone H3. Nat. Commun. 6(1), 8922 (2015). • The authors suggest Rv1988 to be a mycobacterial virulence factor. It methylates histone H3 at H3R42 and perturbs the first line of defence against mycobacteria.