From 837a756553f02f8629c8bda1fa5bd08b747d47c4 Mon Sep 17 00:00:00 2001
From: Aude BERNHEIM <aude.bernheim@pasteur.fr>
Date: Wed, 22 Nov 2023 15:27:41 +0100
Subject: [PATCH] Update rloc.md
---
content/3.defense-systems/rloc.md | 24 ++++++++++++++----------
1 file changed, 14 insertions(+), 10 deletions(-)
diff --git a/content/3.defense-systems/rloc.md b/content/3.defense-systems/rloc.md
index 0ee3e092..bb7a272a 100644
--- a/content/3.defense-systems/rloc.md
+++ b/content/3.defense-systems/rloc.md
@@ -10,9 +10,23 @@ tableColumns:
Activator: Unknown
Effector: Nucleic acid degrading
PFAM: PF13166
+
+contributors:
+ - Aude Bernheim
+relevantAbstracts:
+ - doi: 10.1111/j.1365-2958.2008.06387.x
+
---
# RloC
+
+## Description
+
+RloC is a distant homologue of the tRNALys anticodon nuclease (ACNase) PrrC. RloC shares the ABC ATPase motifs and catalytic ACNase triad with PrrC, but it possesses a unique zinc-hook/coiled-coil insert. This distinctive feature results in its ATPase domain bearing similarity to Rad50 and other DNA repair proteins.Contrary to PrrC RloC is rarely linked to a type I R-M system. RloC activity was not directly demonstrated on phages but hypothesized through its similar features to PrrC :ref{doi=10.1111/j.1365-2958.2008.06387.x}.
+
+## Molecular Mechanism
+RloC was shown to function by tRNA cleavage (wobble nucleotide-excising and Zn++-responsive tRNase) :ref{doi=10.1006/jmbi.1995.0343}. However such activity was not directly shown on a phage. Zinc hook seems to regulate the nuclease function.
+
## Example of genomic structure
The RloC system is composed of one protein: RloC.
@@ -67,14 +81,4 @@ end
style Title3 fill:none,stroke:none,stroke-width:none
style Title4 fill:none,stroke:none,stroke-width:none
</mermaid>
-## Relevant abstracts
-
-::relevant-abstracts
----
-items:
- - doi: 10.1111/j.1365-2958.2008.06387.x
- - doi: 10.1111/mmi.13074
-
----
-::
--
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