Papers of special note have been highlighted as: • of interest; •• of considerable interest
References
- 1. . Nucleosome remodeling and epigenetics. Cold Spring Harb. Perspect. Biol. 5(9), 1–19 (2013).
- 2. . The molecular hallmarks of epigenetic control. Nat. Rev. Genet. 17(8), 487–500 (2016).
- 3. . The winding path of protein methylation research: milestones and new frontiers. Nat. Rev. Mol. Cell Biol. 18(8), 517–527 (2017).
- 4. . 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. . Threonine phosphorylation fine-tunes the regulatory activity of histone-like nucleoid structuring protein in Salmonella transcription. Front. Microbiol. 10, 1515 (2019).
- 6. . 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. . Post-translational modification of nucleoidassociated proteins: an extra layer of functional modulation in bacteria? Biochem. Soc. Trans. 46(5), 1381–1392 (2018).
- 8. . The MycoBrowser portal: a comprehensive and manually annotated resource for mycobacterial genomes. Tuberculosis 91(1), 8–13 (2011).
- 9. . 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. 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. . Lysine acetylation of the Mycobacterium tuberculosis HU protein modulates its DNA binding and genome organization. Mol. Microbiol. 100(4), 577–588 (2016).
- 12. . Rv0802c is an acyltransferase that succinylates and acetylates Mycobacterium tuberculosis nucleoid-associated protein HU. Microbiology 167(7), 001058 (2021).
- 13. 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. . 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. 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. . 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. 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. . 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.