Abstract
A natural fusion occurring between two tandemly repeated glutaredoxin (Grx) modules and a methionine sulfoxide reductase A (MsrA) has been detected in Gracilaria gracilis. Using an in vivo yeast complementation assay and in vitro activity measurements, we demonstrated that this fusion enzyme was able to reduce methionine sulfoxide into methionine using glutathione as a reductant. Consistently, a poplar cytosolic MsrA can be regenerated in vitro by glutaredoxins with an efficiency comparable to that of thioredoxins, but using a different mechanism. We hypothesize that the glutathione/glutaredoxin system could constitute an evolutionary conserved alternative regeneration system for MsrA.
Copyright © 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Amino Acid Sequence
-
Biological Evolution
-
Escherichia coli
-
Genetic Complementation Test
-
Glutaredoxins / genetics
-
Glutaredoxins / metabolism*
-
Glutathione / metabolism*
-
Gracilaria / enzymology*
-
Gracilaria / genetics
-
Kinetics
-
Methionine / analogs & derivatives
-
Methionine / metabolism
-
Methionine Sulfoxide Reductases / genetics
-
Methionine Sulfoxide Reductases / metabolism*
-
Molecular Sequence Data
-
Mutant Chimeric Proteins / genetics
-
Mutant Chimeric Proteins / metabolism*
-
Oxidation-Reduction
-
Populus / enzymology*
-
Populus / genetics
-
Recombinant Proteins
-
Saccharomyces cerevisiae
-
Sequence Alignment
Substances
-
Glutaredoxins
-
Mutant Chimeric Proteins
-
Recombinant Proteins
-
Methionine
-
Methionine Sulfoxide Reductases
-
Glutathione
-
methionine sulfoxide