Identification of disulfide reductases in Campylobacterales: a bioinformatics investigation.

@article{citeulike:2088724, abstract = {Disulfide reductases of host-colonising bacteria are involved in the expression of virulence factors, resistance to drugs, and elimination of toxic compounds. Large-scale genome analyses of 281 prokaryotes identified CXXC and CXXC-derived motifs in each microorganism. The total number of these motifs showed correlations with genome size and oxygen tolerance of the prokaryotes. Specific bioinformatic analyses served to identify putative disulfide reductases in the Campylobacterales Campylobacter jejuni, Helicobacter pylori, Wolinella succinogenes and Arcobacter butzleri which colonise the gastrointestinal tract of higher animals. Three filters applied to the genomes of these species yielded 35, 25, 28 and 34 genes, respectively, encoding proteins with the characteristics of disulfide reductases. Ten proteins were common to the four species, including four belonging to the thioredoxin system. The presence of thioredoxin reductase activities was detected in the four bacterial species by observing dithiobis-2-nitrobenzoic acid reduction with beta-nicotinamide adenine dinucleotide phosphate as cofactor. Phylogenetic analyses of the thioredoxin reductases TrxB(1) and TrxB(2) of the four Campylobacterales were performed. Their TrxB(1) proteins were more closely related to those of Firmicutes than to the corresponding proteins of other Proteobacteria. The Campylobacterales TrxB(2) proteins were closer to glutathione reductases of other organisms than to their respective TrxB(1) proteins. The phylogenetic features of the Campylobacterales thioredoxin reductases suggested a special role for these enzymes in the physiology of these bacteria.}, address = {School of Medical Sciences, The University of New South Wales, Sydney, NSW 2052, Australia.}, author = {Kaakoush, N. O. and Sterzenbach, T. and Miller, W. G. and Suerbaum, S. and Mendz, G. L. }, citeulike-article-id = {2088724}, doi = {10.1007/s10482-007-9171-5}, issn = {0003-6072}, journal = {Antonie Van Leeuwenhoek}, keywords = {2007, bacteria, bioinformatics, comparative\_genomics, genome}, month = {November}, number = {4}, pages = {429--441}, posted-at = {2007-12-11 09:02:55}, priority = {2}, title = {Identification of disulfide reductases in Campylobacterales: a bioinformatics investigation.}, url = {http://dx.doi.org/10.1007/s10482-007-9171-5}, volume = {92}, year = {2007} }

TY - JOUR ID - citeulike:2088724 L3 - citeulike-article-id:2088724 TI - Identification of disulfide reductases in Campylobacterales: a bioinformatics investigation. JF - Antonie Van Leeuwenhoek VL - 92 IS - 4 SP - 429 EP - 441 AD - School of Medical Sciences, The University of New South Wales, Sydney, NSW 2052, Australia. SN - 0003-6072 N2 - Disulfide reductases of host-colonising bacteria are involved in the expression of virulence factors, resistance to drugs, and elimination of toxic compounds. Large-scale genome analyses of 281 prokaryotes identified CXXC and CXXC-derived motifs in each microorganism. The total number of these motifs showed correlations with genome size and oxygen tolerance of the prokaryotes. Specific bioinformatic analyses served to identify putative disulfide reductases in the Campylobacterales Campylobacter jejuni, Helicobacter pylori, Wolinella succinogenes and Arcobacter butzleri which colonise the gastrointestinal tract of higher animals. Three filters applied to the genomes of these species yielded 35, 25, 28 and 34 genes, respectively, encoding proteins with the characteristics of disulfide reductases. Ten proteins were common to the four species, including four belonging to the thioredoxin system. The presence of thioredoxin reductase activities was detected in the four bacterial species by observing dithiobis-2-nitrobenzoic acid reduction with beta-nicotinamide adenine dinucleotide phosphate as cofactor. Phylogenetic analyses of the thioredoxin reductases TrxB(1) and TrxB(2) of the four Campylobacterales were performed. Their TrxB(1) proteins were more closely related to those of Firmicutes than to the corresponding proteins of other Proteobacteria. The Campylobacterales TrxB(2) proteins were closer to glutathione reductases of other organisms than to their respective TrxB(1) proteins. The phylogenetic features of the Campylobacterales thioredoxin reductases suggested a special role for these enzymes in the physiology of these bacteria. KW - 2007 KW - bacteria KW - bioinformatics KW - comparative_genomics KW - genome AU - Kaakoush, NO AU - Sterzenbach, T AU - Miller, WG AU - Suerbaum, S AU - Mendz, GL PY - 2007/11// UR - http://dx.doi.org/10.1007/s10482-007-9171-5 ER -