From f0b4085918a38696adcaab5c50cf28e12d6869ca Mon Sep 17 00:00:00 2001
From: Jean CURY <jean.cury@pasteur.fr>
Date: Wed, 29 Nov 2023 17:32:15 +0100
Subject: [PATCH] Update rloc.md
---
content/3.defense-systems/rloc.md | 3 ++-
1 file changed, 2 insertions(+), 1 deletion(-)
diff --git a/content/3.defense-systems/rloc.md b/content/3.defense-systems/rloc.md
index bb7a272a..791fa1f0 100644
--- a/content/3.defense-systems/rloc.md
+++ b/content/3.defense-systems/rloc.md
@@ -22,9 +22,10 @@ relevantAbstracts:
## 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}.
+RloC is a distant homologue of the tRNALys anticodon nuclease (ACNase) [PrrC](/defense-systems/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
--
GitLab