N-acetylaspartic acid in G-actin

https://doi.org/10.1016/0304-4165(66)90164-4Get rights and content

Abstract

A ninhydrin-negative peptide fraction obtained from pronase digestion of G-actin was isolated on a Dowex-50 X-2 (H+) column. Analysis of this fraction by gas chromatography showed that most of the acetyl content of the original actin was recovered. The presence of an acetyl group in the peptide fraction was also demonstrated by hydrazinolysis. This fraction consists mainly of a tripeptide which, upon degradation with carboxypeptidase A (EC 3.4.2.1, had an amino acid sequence of N-acetyl-Asp-Glu-Thr. It is suggested that N-acetylaspartic acid is the NH2-terminal residue of G-actin.

References (22)

  • H.M.J. Krans et al.

    Biochim. Biophys. Acta

    (1965)
  • R.H. Locker

    Biochim. Biophys. Acta

    (1954)
  • K. Narita

    Biochim. Biophys. Acta

    (1958)
  • K. Narita

    Biochim. Biophys. Acta

    (1959)
  • J.I. Folk et al.

    Biochim. Biophys. Acta

    (1960)
  • G.W. Offer

    Biochim. Biophys. Acta

    (1964)
  • M. Bárány et al.

    Biochim. Biophys. Acta

    (1959)
  • J.A. Winstead et al.

    J. Biol. Chem.

    (1964)
  • S. Moore et al.

    J. Biol. Chem.

    (1954)
  • J.I. Harris

    Biochem. J.

    (1959)
  • K. Narita et al.

    J. Biochem. Tokyo

    (1962)
  • Cited by (26)

    • Actin Post-translational Modifications: The Cinderella of Cytoskeletal Control

      2019, Trends in Biochemical Sciences
      Citation Excerpt :

      However, as described later in this review, there are clear cases of isoform-specific PTMs contributing to differentiated functions. The first actin PTM, N-terminal (Nt) acetylation, was reported for skeletal muscle actin in 1966 by Gaetjens and Bárány [11], and later identified in all other actin isoforms. Today, more than 140 PTMs have been described in eukaryotic actin sequences ([3] and http://www.phosphosite.org).

    View all citing articles on Scopus
    View full text