Secretory Proteins of Chironomus Salivary Glands: Structural Motifs and Assembly Characteristics of a Novel Biopolymer.

摘要

The overall goal of this project has been to learn about the structure, developmentally regulated synthesis and assembly of a family of secretory proteins (SPs) that are synthesized in salivary glands of an aquatic insect and assembled into an insoluble biopolymer of silk-like threads. Molecular biological and immunological techniques were used to ascertain in the structure of two additional SPs and the developmental regulation of the expression of their genes. A 185/220-kDal Cys-rich SP homologue has been identified in three species of Chironomus. Biochemical, biophysical and electron microscopic techniques were used to study SP disassembly/reassembly in vitro and measure the higher order structure of 1000-kDal SPs and their repeated domains in the form of synthetic peptides. This domain approach to protein structure was extended to insect chorions. Eukaryotic genes, secretory polypeptides, tandemly repeated amino acid sequences, in vitro assembly/disassembly of polypeptide fibers, protein-protein interactions