Open AccessThe nucleotide sequence of the Desulfovibrio gigas desulforedoxin gene indicates that the Desulfovibrio vulgaris rbo gene originated from a gene fusion event
Author(s) -
Michael J. Brumlik,
Gisèle Leroy,
Mireille Bruschi,
Gerrit Voordouw
Publication year - 1990
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.172.12.7289-7292.1990
Subject(s) - desulfovibrio vulgaris , biology , gene , gene product , nucleic acid sequence , hspa2 , microbiology and biotechnology , desulfovibrio , peptide sequence , fusion protein , fusion gene , biochemistry , akt1s1 , gene expression , genetics , bacteria , recombinant dna
Expression of the rbo gene from Desulfovibrio vulgaris Hildenborough in Escherichia coli minicells and Western blotting (immunoblotting) of Desulfovibrio cell extracts with antibodies raised against a synthetic peptide indicated the presence of a 14-kDa polypeptide product, as expected from the gene sequence. Cloning and sequencing of the gene (dsr) for desulforedoxin, a 4-kDa redox protein from Desulfovibrio gigas, showed that it is formed by expression of an autonomous gene of 111 bp, not by processing of a 14-kDa protein. The results indicate that the rbo gene product, which has a 4-kDa desulforedoxin domain as the NH2 terminus, may have arisen by gene fusion. Shuffling and fusion of genes for redox protein domains can explain the large variety of redox proteins found in sulfate-reducing bacteria.