Botulinum C2 toxin ADP-ribosylates cytoplasmic beta/gamma-actin in arginine 177

Isolated cytoplasmic actin of human platelet and pig liver actin, but not rabbit skeletal muscle actin, was ADP-ribosylated by botulinum C2 toxin in the presence of [32P]NAD. Tryptic digestion of the [32P]ADP-ribosylated platelet actin generated two labeled peptides: a soluble peptide covering resid...

Full description

Saved in:
Bibliographic Details
Published in:The Journal of biological chemistry 1988-01, Vol.263 (2), p.696-700
Main Authors: Vandekerckhove, J, Schering, B, Bärmann, M, Aktories, K
Format: Article
Language:English
Subjects:
Actins - metabolism
Adenosine Diphosphate Ribose - metabolism
Amino Acid Sequence
Analytical, structural and metabolic biochemistry
Animals
Arginine
Biological and medical sciences
Botulinum Toxins - pharmacology
Clostridium botulinum
Contractile proteins
Cytoplasm - metabolism
Electrophoresis, Polyacrylamide Gel
Fundamental and applied biological sciences. Psychology
Holoproteins
Humans
Isoelectric Focusing
liver
Peptide Mapping
Proteins
Rabbits
Swine
toxins
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Isolated cytoplasmic actin of human platelet and pig liver actin, but not rabbit skeletal muscle actin, was ADP-ribosylated by botulinum C2 toxin in the presence of [32P]NAD. Tryptic digestion of the [32P]ADP-ribosylated platelet actin generated two labeled peptides: a soluble peptide covering residues 174-183 and an insoluble fragment containing residues 148-183. Further digestion of these two peptides with thermolysin yielded the same radioactive peptide, which was in both cases peptide 175-177. Amino acid sequence analysis of peptides 174-183 and 175-177 located the ADP-ribosylation on Arg177.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(19)35408-0