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Resources » Paper

E Jin Shin et al. (2006) East Asia C. elegans Meeting "PDK, a Molecular Switch for Energy Metabolism in Caenorhabditis elegans"

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    Publication type:
    Meeting_abstract
    WormBase ID:
    WBPaper00028702

    E Jin Shin, & Young-Ki Paik (2006). PDK, a Molecular Switch for Energy Metabolism in Caenorhabditis elegans presented in East Asia C. elegans Meeting. Unpublished information; cite only with author permission.

    When faced with an adverse environment such as depletion of food, constitutively secreted C. elegans daumone signals this nematode enter dauer stage, an enduring and non-aged condition. We hypothesized that like hibernating animal C. elegans might also have the same molecular machine which controls an energy consumption during dauer stage. To understand a molecular mechanism by which dauer larvae manage energy metabolism, we were interested in cloning and characterizing C. elegans pyruvate dehydrogenase kinase (CePDK), which has been known as molecular switch for hibernating animal by preventing the flow of glycolytic products into the tricarboxylic acid cycle in the adverse condition. Through the extensive homologue search and molecular cloning works, we isolated ZK370.5 clone which is believed to encode CePDK. Having established that the over-expressed recombinant CePDK in E. coli exhibited the anticipated molecular characteristics such as molecular size and catalytic function, mRNA expression pattern was examined using quantitative RT-PCR. Our preliminary data showed that CePDK mRNA is highly expressed in either dauer or starved state but suppressed in other states, suggesting the presence of regulatory mechanism by which the nutritional state can be sensitized by CePDK in this nematode. When examined mRNA distribution in the several mutants that are grown at fed, starved and dauer condition, the levels of CePDK gene expression were higher in both daf-2 and age-1 than those in either daf-16 or nhr-49. In particular, RNAi of CePDK in daf-2 mutants resulted in a reduced lifespan, indicating that PDK may also be regulated by DAF-16. (Supported by a grant from BioGreen 21 Project to YKP).


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