Evolution and higher-order structure of architectural proteins in silkmoth chorion.

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TitleEvolution and higher-order structure of architectural proteins in silkmoth chorion.
Publication TypeJournal Article
Year of Publication1986
AuthorsRegier, JC
JournalEMBO J
Date Published1986 Aug
KeywordsAmino Acid Sequence, Animals, Base Sequence, Biological Evolution, Chorion, DNA, Egg Proteins, Genes, Lepidoptera, Moths, Repetitive Sequences, Nucleic Acid

Genomic and cDNA clones have been sequenced that encode the E2 silkmoth chorion protein. E2 assembles with E1 [Regier, J.C. and Pacholski, P. (1985) Proc. Natl. Acad. Sci. USA, 82, 6035-6039] to form the 'filler' that helps mold prominent chorion surface structures called aeropyle crowns. E2 has two distinct domains. The amino terminal domain consists of four alternating stretches of hydrophobic and hydrophilic residues, the first three of which are homologous in sequence to about half of the E1 protein. Comparison of predicted secondary structures provides further support for the localized homology of E2 and E1. The carboxy terminal domain of E2 is much longer, is hydrophilic and consists entirely of multiple tandem copies of a single, variant hexapeptide repeat sequence that is absent from E1. Numbers of hexapeptide repeat sequences differed dramatically in two animals. The types of events required for such variation are discussed. Finally, we have elaborated our earlier model for how E proteins may assemble in vivo to form filler.

Alternate JournalEMBO J.
PubMed ID3758029
PubMed Central IDPMC1167067
Grant List1 U41 RR-01685-02 / RR / NCRR NIH HHS / United States