Characterization of a signal peptide sequence in the cell-free translation product of sheep elastin mRNA Academic Article uri icon

Overview

MeSH Major

  • Braces
  • Exercise Therapy
  • Intervertebral Disc
  • Low Back Pain
  • Spinal Diseases

abstract

  • In vitro explant cultures of near-term sheep nuchal ligament secrete tropoelastin of approximate Mr 70,000-72,000 while the elastin cell-free product of sheep nuchal ligament RNA is 2000 to 3000 Mr larger. Automated Edman degradation of immunoprecipitates of radiolabeled cell-free elastin precursor demonstrated the presence of a 26-residue signal sequence which was absent from sheep tropoelastin secreted from explant cultures. In addition, a 20-residue overlap was established between the cell-free product and the secreted protein. This overlap region, representing the N-terminal sequence of ovine tropoelastin, demonstrated complete homology with the N-terminal sequence of porcine tropoelastin and near complete homology with chick tropoelastin. These findings suggest that cotranslational removal of this hydrophobic peptide extension is likely a correlate of vectorial transport of elastin into the secretory apparatus. © 1982.

publication date

  • October 1982

Research

keywords

  • Academic Article

Identity

Digital Object Identifier (DOI)

  • 10.1016/0003-9861(82)90317-4

Additional Document Info

start page

  • 31

end page

  • 7

volume

  • 218

number

  • 1