diff --git a/content/3.defense-systems/rloc.md b/content/3.defense-systems/rloc.md index 0ee3e092756f95b8ab9ee5c253ce1b9ec0ded973..bb7a272a56af76f34ea770eb0a9be985e519be28 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 - ---- -::