Molecular characterization of a novel, developmentally regulated small embryonic chaperone from Caenorhabditis elegans.

The Journal of Biological Chemistry
B LinderC S Rubin

Abstract

Low molecular weight chaperones inhibit protein aggregation and facilitate refolding of partially denatured polypeptides in cells subjected to physical and chemical stresses. The nematode Caenorhabditis elegans provides a system amenable for investigations on roles for chaperone proteins in normal homeostasis and development. We characterized a C. elegans gene and cDNAs that encode a novel, small embryonic chaperone-like protein (SEC-1) that is composed of 159 amino acids. The central core of SEC-1 (residues 45-126) is approximately 40% identical with a corresponding segment of mammalian Hsp27 and alphaB crystallin. Expression of SEC-1 in Escherichia coli confers thermotolerance on the bacterium. SEC-1 mRNA is evident only in C. elegans oocytes and developing embryos. Translation and accumulation of SEC-1 protein is temporally coupled with a prolonged burst of intense protein synthesis and rapid mitogenesis during early embryogenesis. As the rate of protein synthesis decreases during late embryogenesis, levels of SEC-1 and its cognate mRNA decline precipitously. Induction/deinduction of SEC-1 is precisely regulated by intrinsic developmental factors rather than extrinsic stresses. In vivo injection of C. elegans oocytes with an...Continue Reading

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