Cysteine catabolism and cysteine desulfhydrase (CdsH/STM0458) in Salmonella enterica serovar typhimurium.
Cysteine is potentially toxic and can affect diverse functions such as oxidative stress, antibiotic resistance, and swarming motility. The contribution of cysteine catabolism in modulating responses to cysteine has not been examined, in part because the genes have not been identified and mutants lacking these genes have not been isolated or characterized. We identified the gene for a previously described cysteine desulfhydrase, which we designated cdsH (formerly STM0458). We also identified a divergently transcribed gene that regulates cdsH expression, which we designated cutR (formerly ybaO, or STM0459). CdsH appears to be the major cysteine-degrading and sulfide-producing enzyme aerobically but not anaerobically. Mutants with deletions of cdsH and ybaO exhibited increased sensitivity to cysteine toxicity and altered swarming motility but unaltered cysteine-enhanced antibiotic resistance and survival in macrophages.
Department of Molecular and Cell Biology, University of Texas at Dallas, Richardson, Texas, USA.
Tamiko
T
Oguri
Barbara
B
Schneider
Larry
L
Reitzer
D003542:Cystathionine gamma-Lyase / Q000235:genetics / Q000378:metabolism*; D003545:Cysteine / Q000378:metabolism*; D017353:Gene Deletion; D008124:Locomotion; D008264:Macrophages / Q000382:microbiology; D050296:Microbial Viability; D012486:Salmonella typhimurium / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism* / Q000502:physiology
D003542:Cystathionine gamma-Lyase; D003545:Cysteine