TY - JOUR
T1 - Molecular characterization of a novel, developmentally regulated small embryonic chaperone from Caenorhabditis elegans
AU - Linder, Barbara
AU - Jin, Zhijun
AU - Freedman, Jonathan H.
AU - Rubin, Charles S.
PY - 1996
Y1 - 1996
N2 - 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 ~40% identical with a corresponding segment of mammalian Hsp27 and αB 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 antisense oligonucleotides that complement the 5'-end of SEC-1 mRNA arrests nematode development at an early stage after fertilization. Thus, SEC-1 appears to be adapted to perform essential functions in early embryogenesis.
AB - 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 ~40% identical with a corresponding segment of mammalian Hsp27 and αB 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 antisense oligonucleotides that complement the 5'-end of SEC-1 mRNA arrests nematode development at an early stage after fertilization. Thus, SEC-1 appears to be adapted to perform essential functions in early embryogenesis.
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U2 - 10.1074/jbc.271.47.30158
DO - 10.1074/jbc.271.47.30158
M3 - Article
C2 - 8939966
AN - SCOPUS:0029910357
SN - 0021-9258
VL - 271
SP - 30158
EP - 30166
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 47
ER -