ADP-ribosylation of Drosophila indirect-flight-muscle actin and arthrin by Clostridium botulinum C2 toxin and Clostridium perfringens iota toxin

I. Just, E. S. Hennessey, D. R. Drummond, K. Aktories, J. C. Sparrow

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

Purified Drosophila indirect-flight-muscle actin and arthrin, an actin-ubiquitin conjugate, were ADP-ribosylated by Clostridium botulinum C2 toxin and Clostridium perfringens iota toxin. Phalloidin treatment inhibited the ADP-riboyslation of Drosophila actin and arthrin. Like actin, the ADP-ribosearthrin linkage was sensitive towards hydroxylamine treatment, indicating arginine as the amino acid acceptor. Actin translated in vitro from the indirect-flight-muscle-specific gene Act88F was ADP-ribosylated by C. botulinum C2 toxin and C. perfringens iota toxin. Actin from the R177Q mutant of Act88F translated in vivo was not ADP-ribosylated confirming Arg-177 as the ADP-ribose acceptor. Mutant L176M actin was modified by both toxins, indicating that amino acid 176 of actin does not define the substrate specificity of C. botulinum C2 toxin. Whereas the gene products of various C-terminal mutants of Act88F translated in vitro (E334K, V339I, E364K, G368E, R372H) were substrates for ADP-ribosylation by C. botulinum C2 toxin and by C. perfringens iota toxin, neither toxin modified the N-terminal O-12 deletion mutant.

Original languageEnglish
Pages (from-to)409-412
Number of pages4
JournalBiochemical Journal
Volume291
Issue number2
DOIs
Publication statusPublished - Jan 1 1993

Fingerprint

Adenosine Diphosphate
Drosophila
Muscle
Actins
Muscles
Clostridium perfringens
Clostridium
Genes
Adenosine Diphosphate Ribose
Phalloidine
Amino Acids
Hydroxylamine
Substrates
Ubiquitin
Substrate Specificity
arthrin
botulinum toxin type C
Clostridium perfringens iota toxin
Arginine

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

ADP-ribosylation of Drosophila indirect-flight-muscle actin and arthrin by Clostridium botulinum C2 toxin and Clostridium perfringens iota toxin. / Just, I.; Hennessey, E. S.; Drummond, D. R.; Aktories, K.; Sparrow, J. C.

In: Biochemical Journal, Vol. 291, No. 2, 01.01.1993, p. 409-412.

Research output: Contribution to journalArticle

@article{da54ee294fff412fbc57211744ec21b8,
title = "ADP-ribosylation of Drosophila indirect-flight-muscle actin and arthrin by Clostridium botulinum C2 toxin and Clostridium perfringens iota toxin",
abstract = "Purified Drosophila indirect-flight-muscle actin and arthrin, an actin-ubiquitin conjugate, were ADP-ribosylated by Clostridium botulinum C2 toxin and Clostridium perfringens iota toxin. Phalloidin treatment inhibited the ADP-riboyslation of Drosophila actin and arthrin. Like actin, the ADP-ribosearthrin linkage was sensitive towards hydroxylamine treatment, indicating arginine as the amino acid acceptor. Actin translated in vitro from the indirect-flight-muscle-specific gene Act88F was ADP-ribosylated by C. botulinum C2 toxin and C. perfringens iota toxin. Actin from the R177Q mutant of Act88F translated in vivo was not ADP-ribosylated confirming Arg-177 as the ADP-ribose acceptor. Mutant L176M actin was modified by both toxins, indicating that amino acid 176 of actin does not define the substrate specificity of C. botulinum C2 toxin. Whereas the gene products of various C-terminal mutants of Act88F translated in vitro (E334K, V339I, E364K, G368E, R372H) were substrates for ADP-ribosylation by C. botulinum C2 toxin and by C. perfringens iota toxin, neither toxin modified the N-terminal O-12 deletion mutant.",
author = "I. Just and Hennessey, {E. S.} and Drummond, {D. R.} and K. Aktories and Sparrow, {J. C.}",
year = "1993",
month = "1",
day = "1",
doi = "10.1042/bj2910409",
language = "English",
volume = "291",
pages = "409--412",
journal = "Biochemical Journal",
issn = "0264-6021",
publisher = "Portland Press Ltd.",
number = "2",

}

TY - JOUR

T1 - ADP-ribosylation of Drosophila indirect-flight-muscle actin and arthrin by Clostridium botulinum C2 toxin and Clostridium perfringens iota toxin

AU - Just, I.

AU - Hennessey, E. S.

AU - Drummond, D. R.

AU - Aktories, K.

AU - Sparrow, J. C.

PY - 1993/1/1

Y1 - 1993/1/1

N2 - Purified Drosophila indirect-flight-muscle actin and arthrin, an actin-ubiquitin conjugate, were ADP-ribosylated by Clostridium botulinum C2 toxin and Clostridium perfringens iota toxin. Phalloidin treatment inhibited the ADP-riboyslation of Drosophila actin and arthrin. Like actin, the ADP-ribosearthrin linkage was sensitive towards hydroxylamine treatment, indicating arginine as the amino acid acceptor. Actin translated in vitro from the indirect-flight-muscle-specific gene Act88F was ADP-ribosylated by C. botulinum C2 toxin and C. perfringens iota toxin. Actin from the R177Q mutant of Act88F translated in vivo was not ADP-ribosylated confirming Arg-177 as the ADP-ribose acceptor. Mutant L176M actin was modified by both toxins, indicating that amino acid 176 of actin does not define the substrate specificity of C. botulinum C2 toxin. Whereas the gene products of various C-terminal mutants of Act88F translated in vitro (E334K, V339I, E364K, G368E, R372H) were substrates for ADP-ribosylation by C. botulinum C2 toxin and by C. perfringens iota toxin, neither toxin modified the N-terminal O-12 deletion mutant.

AB - Purified Drosophila indirect-flight-muscle actin and arthrin, an actin-ubiquitin conjugate, were ADP-ribosylated by Clostridium botulinum C2 toxin and Clostridium perfringens iota toxin. Phalloidin treatment inhibited the ADP-riboyslation of Drosophila actin and arthrin. Like actin, the ADP-ribosearthrin linkage was sensitive towards hydroxylamine treatment, indicating arginine as the amino acid acceptor. Actin translated in vitro from the indirect-flight-muscle-specific gene Act88F was ADP-ribosylated by C. botulinum C2 toxin and C. perfringens iota toxin. Actin from the R177Q mutant of Act88F translated in vivo was not ADP-ribosylated confirming Arg-177 as the ADP-ribose acceptor. Mutant L176M actin was modified by both toxins, indicating that amino acid 176 of actin does not define the substrate specificity of C. botulinum C2 toxin. Whereas the gene products of various C-terminal mutants of Act88F translated in vitro (E334K, V339I, E364K, G368E, R372H) were substrates for ADP-ribosylation by C. botulinum C2 toxin and by C. perfringens iota toxin, neither toxin modified the N-terminal O-12 deletion mutant.

UR - http://www.scopus.com/inward/record.url?scp=0027269530&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027269530&partnerID=8YFLogxK

U2 - 10.1042/bj2910409

DO - 10.1042/bj2910409

M3 - Article

C2 - 8484722

AN - SCOPUS:0027269530

VL - 291

SP - 409

EP - 412

JO - Biochemical Journal

JF - Biochemical Journal

SN - 0264-6021

IS - 2

ER -