Proteomic analysis of the effect of cyanide on Klebsiella oxytoca.
Cyanide has been proved to be degraded by Klebsiella oxytoca. In order to examine the physiological responses of cyanide degradation by this bacterium, two-dimensional (2-DE) electrophoresis approach and MALDI-TOF-MS allow us to identify 106 proteins spots that were significantly altered in the presence of 1 mM cyanide in relative to that in 1 mM ammonia when K. oxytoca grown at the late-log phase. Among them, 27 proteins were successfully identified. These proteins were involved in carbohydrate metabolism, nucleotide metabolism, amino acid metabolism, nitrogen metabolism, stress responses, oxidation-reduction reactions, transporters, and miscellaneous function. Some proteins related with regulation of nitrogen assimilation pathways (glutamine synthetase), oxidative stress repairing (catalase), and protection (neutral trehalase and glycosyltransferase) could improve the effectiveness of cyanide biodegradation. Although the nitrogenase was suggested to participate in cyanide degradation in our previous study, this enzyme induction was not observed as expected. These findings could provide new insights into the inducible mechanisms underlying the capacity of K. oxytoca to tolerate cyanide stress.
Tang
Petrus
P
Bioinformatics Center, Chang Gung University, Taoyuan, Taiwan, ROC.
Hseu
You-Cheng
YC
Chou
Hui-Hsuan
HH
Huang
Kuo-Yang
KY
Chen
Ssu Ching
SC
D001426:Bacterial Proteins / Q000187:drug effects / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D003486:Cyanides / Q000494:pharmacology*; D015536:Down-Regulation / Q000187:drug effects; D015180:Electrophoresis, Gel, Two-Dimensional / Q000379:methods; D007700:Kinetics; D041121:Klebsiella oxytoca / Q000187:drug effects / Q000235:genetics* / Q000254:growth & development; D040901:Proteomics / Q000379:methods*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D015854:Up-Regulation / Q000187:drug effects
D001426:Bacterial Proteins; D003486:Cyanides