The role of DmsD in the biosynthesis of dimethyl sulfoxide (DMSO) reductase is quite controversial. Several studies have indicated its role as ‘proof-reading chaperone’, which might function to prevent the translocation of misfolded and non-cofactor containing protein. DmsD is also shown to bind to the signal peptide; however, its possible function as a ‘guidance factor’ for membrane targeting is ruled out by some experimental evidences. In this computational study, the interactions of DmsD with some other proteins were analyzed. The results of the analysis indicate that rather than playing the role of a chaperone directly, DmsD may influence the recruitment of GroEL, MoeB, and DnaK which can function as a chaperone for protein folding. The results of this analysis were also used together with the findings of available literature to generate a hypothetical model, proposing a possible function of DmsD in the biosynthesis of DMSO reductase.
Key words: Dimethyl sulfoxide (DMSO) reductase, DmsD, molecular docking.
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