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Published January 1, 1978 | public
Journal Article Open

Silkmoth chorion proteins: Sequence analysis of the products of a multigene family


Five polypeptide components have been isolated from the eggshell (chorion) of a silkmoth. Two are homogeneous on sodium dodecyl sulfate and isoelectric focusing gels, and three contain predominantly two proteins each. Amino acid analyses show that all five components are similar to each other. These proteins have been sequenced from the amino terminus. Homogeneous components yielded single sequences; heterogeneous components yielded two residues at some positions, consistent with their containing two major electrophoretic components. Striking similarities are apparent among all these sequences. These similarities can be increased dramatically by separating each of the three protein mixtures into two sequences and introducing a small number of gaps or insertions. This is due in part to bringing into register a portion that contains short repeating subunits found in all sequences. All proteins are also characterized by a region of high cysteine content near the amino terminus followed by a longer low-cysteine region. The data suggest that these proteins share a common evolutionary origin and are encoded by a multigene family.

Additional Information

© 1978 by the National Academy of Sciences. Communicated by E. B. Lewis, September 2, 1977. We thank M. Koehler for patient help with the figures and M. Randell for expert secretarial assistance. This work was supported by grants from the National Science Foundation and the National Institutes of Health to F.C.K. and to L.H. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.


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