ADP-ribosyl proteins formed by pertussis toxin are specifically cleaved by mercury ions

Biol Chem Hoppe Seyler. 1988 Jul;369(7):579-83. doi: 10.1515/bchm3.1988.369.2.579.

Abstract

Various types of ADP-ribosyl protein conjugates were synthesized and their chemical stability was compared with that of cysteine-linked ADP-ribosyl groups as formed by incubation of transducin or Gi/Go proteins with NAD and pertussis toxin. Treatment with 0.1 mM HgCl2 specifically cleaved the cysteine-linked conjugates. This may provide a tool for the quantitation of modified Gi/Go proteins as well as of other acceptors modified by ADP-ribose at cysteine residues in the presence of other ADP-ribosyl proteins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Diphosphate Ribose / metabolism*
  • Animals
  • Cattle
  • Cysteine
  • Histones / metabolism*
  • Hydrolysis
  • Mercury / pharmacology*
  • Mitochondria, Heart / metabolism
  • NAD / metabolism
  • Peptide Elongation Factor 2
  • Peptide Elongation Factors / metabolism
  • Peptides / metabolism*
  • Pertussis Toxin*
  • Proteins / metabolism*
  • Submitochondrial Particles / metabolism
  • Transducin / metabolism
  • Virulence Factors, Bordetella / metabolism*

Substances

  • Histones
  • Peptide Elongation Factor 2
  • Peptide Elongation Factors
  • Peptides
  • Proteins
  • Virulence Factors, Bordetella
  • NAD
  • Adenosine Diphosphate Ribose
  • Pertussis Toxin
  • Transducin
  • Mercury
  • Cysteine