Genetic variants of the Bombyx mori silkworn encoding sericin proteins of different lengths.
A variant sericin polypeptide originally found by acid gel electrophoresis in the Nd-s mutant strain of the silkworm, Bombyx mori, has been analyzed genetically. The variant polypeptide (called S-2v) is encoded by a gene which behaves as a codominant allele of the gene encoding the standard S-2 sericin polypeptide. Linkage analysis locates these alleles at 0.0 map unit on chromosome 11. SDS-polyacrylamide gel electrophoresis shows that the molecular weight of the S-2v variant polypeptide is lower by approximately 62,500 than that of the S-2 polypeptide. Amino acid analysis indicates that the two sericin polypeptides have similar compositions. These results are consistent with the idea that the variant allele arose by deletion within the S-2 coding sequence in the Src-2 gene locus as the result of unequal recombination.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D012831:Bombyx / Q000235:genetics*; D002874:Chromosome Mapping; D004591:Electrophoresis, Polyacrylamide Gel; D005796:Genes; D005799:Genes, Dominant; D008970:Molecular Weight; D009154:Mutation; D010456:Peptides, Cyclic / Q000032:analysis / Q000235:genetics*; D047030:Sericins
D000596:Amino Acids; D010456:Peptides, Cyclic; D047030:Sericins