Alignment of the peptides derived from acid-catalyzed cleavage of an aspartylprolyl bond in the major internal structural polypeptide of avian retroviruses

Academic Article

Abstract

  • The major internal structural polypeptide (p27) of Rous sarcoma virus (RSV), and the analogous polypeptide (p270) of Rous-associated virus-O (RAV-O), an endogenous virus released spontaneously by some chicken cells) have been cleaved selectively at a single aspartylprolyl peptide bond to yield two fragments. The NH2- and COOH-terminal amino acid sequences of p27 and p270 and their mild acid-cleavage fragments have been determined. These results show the existence of an identical cleavage site and a similar NH2- and COOH-terminal amino acid sequence in both the poly-peptides. Furthermore they indicate that the difference in the molecular weights of p27 and p270 results from an insertion of amino acids in the COOH-terminal peptide of p270 rather than a shift in the scission site of the precursor molecule.
  • Authors

    Published In

    Pubmed Id

  • 8537364
  • Author List

  • Bhown AS; Bennett JC; Hunter E
  • Start Page

  • 6962
  • End Page

  • 6965
  • Volume

  • 255
  • Issue

  • 14