Disease relevance of msrA

• The wild-type phenotype was restored by transformation with plasmids encoding msrA from E. coli or M. tuberculosis, but not by an enzymatically inactive mutant msrA, indicating that Met oxidation was involved in the death of these cells [1].

High impact information on msrA

• In the pms mutant background, all phenotypes caused by the mmsA mutation were attenuated [2].
• Therefore, the pms mutation, although it affected mismatch repair and, to some extent, DNA repair and recombination, acted as a suppressor of the mmsA mutation [2].
• Solution Structure and Backbone Dynamics of the Reduced Form and an Oxidized Form of E. coli Methionine Sulfoxide Reductase A (MsrA): Structural Insight of the MsrA Catalytic Cycle [3].
• The Arabidopsis plastidic methionine sulfoxide reductase B proteins. Sequence and activity characteristics, comparison of the expression with plastidic methionine sulfoxide reductase A, and induction by photooxidative stress [4].
• (1)H, (13)C and (15)N Resonance Assignment of an Oxidized form (Cys(51)-Cys (198)) of Methionine Sulfoxide Reductase A from Escherichia Coli [5].

Chemical compound and disease context of msrA

• Employing a msrA/B double mutant, a new peptide methionine sulfoxide reductase activity has been found associated with membrane vesicles from E. coli [6].

Biological context of msrA

• Yet, the recent identification of a direct link between protein targeting and MsrA/MsrB repair offers a best illustration of the physiological importance of this pathway [7].

Associations of msrA with chemical compounds

• Recent years have brought a wealth of new information on methionine sulfoxide reductase A (MsrA) and B (MsrB) which makes methionine oxidation a reversible process [7].

References