Abstract
A locus responsible for the Nd-s mutation of the silkworm, Bombyx mori, has been mapped very close to or within the fibroin light (L) chain gene on the 14th chromosome (Takei, F., K. Kimura, S. Mizuno, T. Yamamoto, and K. Shimura, 1984, Jpn. J. Genet., 59:307-313). A strain of B. mori carrying the homozygous Nd-sD mutation (Nd-sD/Nd-sD; Nd-sD is allelic to Nd-s) secretes less than 0.3% of fibroin into the lumen of the posterior silk gland compared with a strain carrying the homozygous wild-type alleles (+/+). The small amount of fibroin that is secreted in the Nd-sD/Nd-sD strain consists of the heavy (H) chain only and lacks the L chain, although the L chain mRNA and the proteins that are cross-reactable with the anti-L chain serum are present in the posterior silk gland cells. In the hybrid silkworm, Nd-sD/+, the H chain derived from either the Nd-sD or + allele forms disulfide linkage with the L chain derived from the + allele and these fibroins are secreted into the lumen with an equal efficiency, but the L chain derived from the Nd-sD allele remains in the cell unbound to the H chain. Some evidence suggesting structural abnormality of the L chain derived from the Nd-sD allele is presented. These results, together with the previous results on the effect of the H chain gene-linked Nd(2) mutation (Takei, F., F. Oyama, K. Kimura, A. Hyodo, S. Mizuno, and K. Shimura, 1984, J. Cell Biol., 99:2005-2010), strongly suggest that the H-L subunit combination of silk fibroin is important for its efficient secretion.
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