Hybridization-selected translation of Bombyx mori high-cysteine chorion proteins in Xenopus laevis oocytes.

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Abstract
X. laevis oocytes were injected with poly(A)+-mRNA isolated from chorionating follicular epithelium of the domesticated silk moth (B. mori). On 2-dimensional gel electrophoresis, the resultant translation products comigrated with authentic, secreted, chorion standards, demonstrating that the frog oocyte system synthesizes and correctly processes virtually all major chorion components. A c[complementary]DNA clone was shown to contain sequences complementary to those of mRNA encoding B. mori high-cysteine (Hc) chorion proteins Hc6-Hc11. mRNA were selected by hybridization to plasmid m5000 DNA bound to diazobenzyloxymethyl-cellulose and subsequently translated in X. laevis oocytes into forms that comigrated with authentic chorion standards. The selection of a distinct subset of Hc mRNA under stringent hybridization conditions (70% formamide/0.2 M NaCl, 60.degree. C) suggests they are encoded by related genes. This is consistent with the pattern obtained by hybridizing radioactive m5000 DNA to Southern blots prepared from EcoRI-cleaved B. mori chromosomal DNA.