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|Type of Document
||A proteomic analysis of Klebsiella oxytoca SYSU-011 after exposure to tetracyanonickelate(II)|
|Date of Defense
||Klebsiella oxytoca SYSU-011 isolated from wastewater of a|
metal-plating plant in southern Taiwan had been proven to be able to
degrade cyanide. In this study, we performed proteomic analyses to
understand the mechanism of tetracyanonickelate (TCN) resistance in K.
oxytoca by using two-dimensional polyacrylamide gel electrophoresis (2-D
PAGE) and MALDI-TOF-MS techniques. There were 91 protein spots had
been induced or overexpressed (≥2 fold) by TCN. Among them, 44 protein
spots were successfully identified by MALDI-TOF-MS. The expressed
proteins that had been escalated including chaperone, glutathione
S-transferase (GST) and alkyl hydroperoxide reductase (AHR) were
involved in the TCN detoxification process. Fructose-bisphosphate aldolase,
glyceraldehyde-3-phosphate dehydrogenase, phosphoglucomutase and
6-phosphogluconolactonase were involved in energy-producing process;
nitrogenase and glutamine synthetase (GS) were required to regulate
nitrogen assimilation. We also analyzed the K. oxytoca membrane proteins.
Twenty six proteins spots had been successfully identified by
MALDI-TOF-MS (out of 41 protein) that were induced ≥2 fold by TCN.
These proteins induced RND-drive efflux proteins (RND family, MFP
subunit, outer membrane factor A and outer membrane factor TolC) and cation efflux system. These efflux pumps could transport nickel ion out of
the cells. The induced ATP-binding cassette (ABC) proteins may also play a
role in transportation of metal-cyano complexes TCN and nutrition.
By this study, we had a better understanding on the defense mechanism
of K. oxytoca after exposure to TCN.
||Chih-Ming Kao - chair|
Chan-Shing Lin - co-chair
Jong-Kang Liu - advisor
Ssu-Ching Chen - advisor
indicate in-campus access in a year and off_campus not accessible|
|Date of Submission