Degradation of transgene-coded and endogenous proteins in the muscles of Caenorhabditis elegans.

Abstract

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.

• Authors: Jennifer L Fostel, Lauren Benner Coste, Lewis A Jacobson
• Journal: Biochemical and biophysical research communications (Biochem Biophys Res Commun) Vol. 312 Issue 1 Pg. 173-7 (Dec 05 2003) ISSN: 0006-291X [Print] United States
• PMID: 14630038 (Publication Type: Journal Article, Research Support, U.S. Gov't, Non-P.H.S.)

Chemical References

• Muscle Proteins
• Recombinant Fusion Proteins
• Arginine Kinase
• Adenylate Kinase
• beta-Galactosidase

Topics

• Adenylate Kinase (chemistry, metabolism)
• Animals
• Animals, Genetically Modified (metabolism)
• Arginine Kinase (chemistry, metabolism)
• Biodegradation, Environmental
• Biotransformation
• Caenorhabditis elegans (genetics, metabolism)
• Gene Expression Regulation (physiology)
• Hydrolysis
• Muscle Proteins (chemistry, metabolism)
• Muscle, Skeletal (metabolism)
• Myofibrils (metabolism)
• Recombinant Fusion Proteins (chemistry, metabolism)
• Starvation (metabolism)
• beta-Galactosidase (chemistry, genetics, metabolism)