Skip to content
Snippets Groups Projects
Commit 1b2ff506 authored by Jean  CURY's avatar Jean CURY
Browse files

start working gaps6.md

parent 6ee8d98d
No related branches found
No related tags found
1 merge request!60start working gaps6.md
Pipeline #116381 passed
......@@ -6,11 +6,25 @@ tableColumns:
doi: 10.1101/2023.03.28.534373
abstract: |
Bacteria are found in ongoing conflicts with rivals and predators, which lead to an evolutionary arms race and the development of innate and adaptive immune systems. Although diverse bacterial immunity mechanisms have been recently identified, many remain unknown, and their dissemination within bacterial populations is poorly understood. Here, we describe a widespread genetic element, defined by the Gamma-Mobile-Trio (GMT) proteins, that serves as a mobile bacterial weapons armory. We show that GMT islands have cargo comprising various combinations of secreted antibacterial toxins, anti-phage defense systems, and secreted anti-eukaryotic toxins. This finding led us to identify four new anti-phage defense systems encoded within GMT islands and reveal their active domains and mechanisms of action. We also find the phage protein that triggers the activation of one of these systems. Thus, we can identify novel toxins and defense systems by investigating proteins of unknown function encoded within GMT islands. Our findings imply that the concept of defense islands may be broadened to include other types of bacterial innate immunity mechanisms, such as antibacterial and anti-eukaryotic toxins that appear to stockpile with anti-phage defense systems within GMT weapon islands.
relevantAbstract:
- doi: 10.1101/2023.03.28.534373
contributors :
- Jean Cury
---
# GAPS6
## To do
## Description
GAPS (GMT-encoded Anti-Phage System) antiphage systems were discovered on newly described Gamma-Mobile-Trio elements.
GAPS6 comprises two genes encoding WP_248387294.1 (GAPS6a) and WP_248387295.1 258 (GAPS6b) (Fig. 6a). These two proteins are encoded together in diverse Gram-negative 259 bacteria
## Molecular mechanism
Predicted structures in the original paper, show that GAPS4a and GAPS4b might interact and form a heterodimer. They suggest that GAPS4 binds to DNA.
GAPS4 is suggested to be an abortive infection system degrading host cell DNA upon phage infection.
## Structure
......@@ -57,11 +71,3 @@ end
style Title3 fill:none,stroke:none,stroke-width:none
style Title4 fill:none,stroke:none,stroke-width:none
</mermaid>
## Relevant abstract
::relevant-abstracts
---
items:
- doi: 10.1101/2023.03.28.534373
---
::
0% Loading or .
You are about to add 0 people to the discussion. Proceed with caution.
Finish editing this message first!
Please register or to comment