title: Mutation study of DsrM from Allochromatium vinosum using the amino acid sequences.
abstract: Sulfur metabolism is one of the oldest known environmental processes. The operon involved in this process is called the dsr operon. The vital role of the operon is to maintain the environmental sulfur balance. The dsr operon of proteobacteria consists of 15 genes, viz. dsrABEFHCMKLJOPNRS. The proteins encoded by the dsr operon are essential for the transfer of sulfur globules from periplasm to cytosol and oxidation of the stored sulfur. In the present study we tried to analyze the probable molecular details of the DsrM proteins from a diverse set of microbial species using their sequence information. There are certain mutations in the sequences of the DsrM proteins from the different proteobacterial species. The effects of mutations in the sequences of DsrM proteins were predicted from the evolutionary point of view. This is so far the first report of its kind. Our study would therefore enable the researches to predict the hitherto unknown biochemistry of sulfur oxidation using the amino acid sequences of the DsrM proteins.
authors.affiliation: Department of Biochemistry and Biophysics, University of Kalyani, Kalyani, Nadia741235, India.
authors.forename: Semanti
authors.initials: S
authors.lastname: Ghosh
authors.affiliation: Department of Biochemistry and Biophysics, University of Kalyani, Kalyani, Nadia741235, India.
authors.forename: Angshuman
authors.initials: A
authors.lastname: Bagchi
keywords: Domain analysis; DsrM protein; Mutation study; Sequence alignment; dsr operon