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Histone methyltransferase SUV39H1 participates in host defense by methylating mycobacterial histone-like protein HupB.

Authors
  • Yaseen, Imtiyaz1, 2
  • Choudhury, Mitali3
  • Sritharan, Manjula3
  • Khosla, Sanjeev4
  • 1 Centre for DNA Fingerprinting and Diagnostics (CDFD), Hyderabad, India. , (India)
  • 2 Graduate Studies, Manipal University, Manipal, India. , (India)
  • 3 Department of Animal Biology, University of Hyderabad, Hyderabad, India. , (India)
  • 4 Centre for DNA Fingerprinting and Diagnostics (CDFD), Hyderabad, India [email protected] , (India)
Type
Published Article
Journal
The EMBO Journal
Publisher
EMBO
Publication Date
Jan 17, 2018
Volume
37
Issue
2
Pages
183–200
Identifiers
DOI: 10.15252/embj.201796918
PMID: 29170282
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

Host cell defense against an invading pathogen depends upon various multifactorial mechanisms, several of which remain undiscovered. Here, we report a novel defense mechanism against mycobacterial infection that utilizes the histone methyltransferase, SUV39H1. Normally, a part of the host chromatin, SUV39H1, was also found to be associated with the mycobacterial bacilli during infection. Its binding to bacilli was accompanied by trimethylation of the mycobacterial histone-like protein, HupB, which in turn reduced the cell adhesion capability of the bacilli. Importantly, SUV39H1-mediated methylation of HupB reduced the mycobacterial survival inside the host cell. This was also true in mice infection experiments. In addition, the ability of mycobacteria to form biofilms, a survival strategy of the bacteria dependent upon cell-cell adhesion, was dramatically reduced in the presence of SUV39H1. Thus, this novel defense mechanism against mycobacteria represents a surrogate function of the epigenetic modulator, SUV39H1, and operates by interfering with their cell-cell adhesion ability. © 2017 The Authors.

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