Biphenyl- and carvone-induced protein expression patterns in Rhodococcus sp. ACS

Abstract

Protein expression patterns in the polychlorinated biphenyl (PCB)-degrading Rhodococcussp. strain ACS were examined following growth on two substrates capable of inducing the enantioselective biotransformation of PCBs via different degradation pathways. Eleven
inducible proteins were identified by SDS-PAGE and characterized by LC-MS/MS. Four of the peptides, a spore coat protein, an extracellular serine protease, a spoVP, and a molecular chaperonin from Bacillus subtilis, were identified as being unique to biphenyl-induced cells, whereas anextracellular serine protease from B. subtilis was identified as being unique to carvone-induced cells.
None of the peptides identified had sequences that corresponded to known dioxygenases or other PCB-degrading enzymes of this Gram- positive bacterium, suggesting that the identified induced proteins may be involved in either PCB degradation or adaptive responses that protect cells from toxicity.


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J. Kim, "Biphenyl- and carvone-induced protein expression patterns in Rhodococcus sp. ACS," Journal of Agricultural Chemistry and Environment, Vol. 2 No. 3, 2013, pp. 65-73. doi: 10.4236/jacen.2013.23010.

Conflicts of Interest

The authors declare no conflicts of interest.

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