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Structural insights into the mechanism of adaptive ribosomal modification by PseudomonasRimK.

Authors :
Thompson, Catriona M. A.
Little, Richard H.
Stevenson, Clare E. M.
Lawson, David M.
Malone, Jacob G.
Source :
Proteins; Mar2023, Vol. 91 Issue 3, p300-314, 15p
Publication Year :
2023

Abstract

Bacteria are equipped with a diverse set of regulatory tools that allow them to quickly adapt to their environment. The RimK system allows for Pseudomonas spp. to adapt through post‐transcriptional regulation by altering the ribosomal subunit RpsF. RimK is found in a wide range of bacteria with a conserved amino acid sequence, however, the genetic context and the role of this protein is highly diverse. By solving and comparing the structures of RimK homologs from two related but functionally divergent systems, we uncovered key structural differences that likely contribute to the different activity levels of each of these homologs. Moreover, we were able to clearly resolve the active site of this protein for the first time, resolving binding of the glutamate substrate. This work advances our understanding of how subtle differences in protein sequence and structure can have profound effects on protein activity, which can in turn result in widespread mechanistic changes. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
08873585
Volume :
91
Issue :
3
Database :
Complementary Index
Journal :
Proteins
Publication Type :
Academic Journal
Accession number :
161657473
Full Text :
https://doi.org/10.1002/prot.26429