[feed] Atom [feed] RSS 1.0 [feed] RSS 2.0

Yaseen, Imtiyaz and Choudhury, Mitali and Sritharan, Manjula and Khosla, Sanjeev (2018) Histone methyltransferase SUV39H1 participates in host defense by methylating mycobacterial histone‐like protein HupB. The EMBO Journal, 37 (2). pp. 183-200. ISSN 1460-2075

[img] Text
EMBO J 37 p183.pdf
Restricted to Repository staff only

Download (2781Kb) | Request a copy

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.

Item Type: Article
Depositing User: Users 2 not found.
Date Deposited: 28 Nov 2017 19:03
Last Modified: 25 Jan 2018 05:33
URI: http://cdfd.sciencecentral.in/id/eprint/815

Actions (login required)

View Item View Item