Secretary Polypeptides Encoded by Balbiani Ring Genes

Abstract

The aim of this project is to learn about the structure, developmentally regulated synthesis and assembly of a family of secretory proteins (SPs) into an insoluble polymer of silk-like threads. SPs are exclusively synthesized in salivary glands of aquatic larvae of the Dipteran, Chironomus. All SPs studied to date are composed of tandemly repeated amino acid sequences. Recombinant cDNA probes are used to map SP-coding genes on polytene chromosomes, identify their mRNAs on Northern blots and derive the amino acid sequence of their encoded protein. This experimental system provides a unique opportunity to study how naturally occurring soluble proteins can assemble into an insoluble fiber that functions in an aqueous environment. Keywords: Eukaryotic genes, Secretory proteins, Tandemly repeated amino acid sequences, In vitro assembly/disassembly of polypeptide fibers, Protein-protein interactions.

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Document Details

Document Type
Technical Report
Publication Date
May 04, 1989
Accession Number
ADA207909

Entities

People

  • Steven T. Case

Organizations

  • University of Mississippi Medical Center

Tags

Communities of Interest

  • Biomedical

DTIC Thesaurus Topics

  • Acids
  • Amino Acids
  • Antibodies
  • Assembly
  • Availability
  • Biochemistry
  • Chemistry
  • Chromosomes
  • Classification
  • Electron Microscopes
  • Electron Microscopy
  • Gene Expression
  • Mississippi
  • Protein-Protein Interactions
  • Salivary Glands
  • Security
  • Spatial Distribution

Fields of Study

  • Biology

Readers

  • Molecular Genetics
  • Molecular and Cellular Biochemistry