Degradation of transgene-coded and endogenous proteins in the muscles of Caenorhabditis elegans.
To develop reporter systems to study the regulation of protein degradation in innervated muscle, we have used strains of the nematode Caenorhabditis elegans containing transgenes that fuse lacZ or green fluorescent protein (GFP) coding regions to muscle-specific promoter/enhancer regions, such that the fusion proteins are expressed exclusively in body-wall and vulval muscle cells. The starvation-induced degradation of the beta-galactosidase reporter protein is quantitatively similar to that of two endogenous muscle proteins, arginine kinase and adenylate kinase. A soluble GFP in the muscle cytosol is degraded during starvation, but when GFP is fused to a full-length myosin heavy chain and incorporated into myofibrils, it is resistant to starvation-induced degradation. This suggests that under some conditions soluble muscle proteins may be extensively catabolized in preference to the proteins of the contractile fibers.[1]References
- Degradation of transgene-coded and endogenous proteins in the muscles of Caenorhabditis elegans. Fostel, J.L., Benner Coste, L., Jacobson, L.A. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
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