Clostridial ADP-ribosyltransferases ? Modification of low molecular weight GTP-binding proteins and of actin by clostridial toxins

Aktories, Klaus

doi:10.1007/bf00202390

Cited by 20 publications

(11 citation statements)

References 92 publications

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“…The F-actin thus prepared from Bpj-actin was transferred to the ADP-ribosylation system containing labelled NAD. In contrast to the data obtained with bacterial toxin (Aktories, 1990), F-actin was ADP ribosylated by chicken transferase. The ADP ribosylation of F-actin was in a time-dependent manner (Fig.…”

Section: Adp Ribosylation Of F-actinscontrasting

confidence: 99%

“…It should be emphasized that chicken ADP-ribosyltransferase modified F-actin while bacterial toxins did not (Aktories et al, 1986a;Aktories, 1990). We presume that this difference may be related to the different arginine site(s) ADP ribosylated by the enzyme and by the toxin.…”

Section: Discusslonmentioning

confidence: 76%

“…Concerning kinetic parameters, bacterial toxin has an optimal pH at 5.5 -6.0 (Just et al, 1990), while the heterophil enzyme is optimal at pH 8.5. The K , value for NAD was calculated to be 1 -5 pM (Aktories et al, 1986b;1990) with C. botulinum C2 toxin, while the value obtained with the heterophil enzyme showed a 10 -20-fold higher value. ADP -ribose incorporated/mol ply-actin was 1 mol for C2 toxin (Ohishi et al, 1990) and the modification site was identified to be Arg177 (Vandekerckhove et al, 1987;1988).…”

Section: Discusslonmentioning

confidence: 99%

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ADP‐ribosylation of actins by arginine‐specific ADP‐ribosyltransferase purified from chicken heterophils

Terashima

Mishima

Yamada

et al. 1992

European Journal of Biochemistry

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We reported the purification and characterization of an arginine-specific ADP-ribosyltransferase and acceptor protein p33 in granules of chicken peripheral polymorphonuclear leukocytes (heterophils) [Mishima, K., Terashima, M., Obara, S.,In the present study, we obtained evidence that chicken non-muscle Ply-actin, skeletal muscle a-actin and smooth-muscle y-actin were ADP ribosylated by the heterophil ADP-ribosyltransferase. The stoichiometry of ADP -ribose incorporation into these actins was 3.2 mol, 1.0 mol and 2.0 mol ADP -ribose/mol of Ply-actin, a-actin and y-actin, respectively. The optimal pH for the ADP ribosylation was at pH 8.5, with the respective actin. K,,, values for NAD were calculated to be 30 pM with B/y-actin, 35 pM with a-actin and 20 pM with y-actin. The K , values for the actin isoforms were 15 pM for j/y-actin, 2.5 pM for a-actin and 10 pM for y-actin. ADP ribosylation of actin inhibited its capacity to polymerize, as determined by the increase in fluoresence intensity with N-(1 -pyrenyl)iodoacetamide-labelled actin. Filamentous actin (F-actin) polymerized with the respective actin isoform was also ADP ribosylated, although the extent of the modification of F-actin was lower than that of globular actin (G-actin). In situ ADP ribosylation of Ply-actin was evidenced with chicken peripheral heterophils permeabilized with saponin. Thus, the endogenous ADP ribosylation of actin in the heterophils may be involved in the cellular processes such as phagocytosis, secretion and migration.

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Section: Adp Ribosylation Of F-actinscontrasting

confidence: 99%

Section: Discusslonmentioning

confidence: 76%

Section: Discusslonmentioning

confidence: 99%

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ADP‐ribosylation of actins by arginine‐specific ADP‐ribosyltransferase purified from chicken heterophils

Terashima

Mishima

Yamada

et al. 1992

European Journal of Biochemistry

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“…In cells o f vertebrates, Clostridium botulinum exoenzyme C3 inhibits the biological activity of small GTP-binding proteins of the rho-gene family by ADP-ribosylation but apparently does not block their G D P-G TP exchange [13,21]. Sub strates for ADP-ribosylation have been found in photoreceptors of vertebrates [14].…”

Section: Injection O F Exoenzym E Cmentioning

confidence: 99%

“…M oreover, the experiments suggest that Limulus photoreceptors contain small GTP-binding proteins (2 0 -3 0 kD a) which are known substrates for A D P-ribosylation by exoenzyme C3 [13] and also seem to take part in or influence the light-activated phototransduc tion cascade of vertebrate photoreceptors [14].…”

Section: Introductionmentioning

confidence: 99%

Disturbing Gtp-Binding Protein Function Through Microinjection Into The Visual Cell Of Limulus

Stieve

Niemeyer

Aktories

et al. 1992

Zeitschrift Für Naturforschung C

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Actin‐ADP‐Ribosylating Toxins: Cytotoxic Mechanisms ofClostridium botulinumC2 Toxin andClostridium perfringenslota Toxin

Aktories¹,

Sehr²,

Just³

1997

Bacterial Toxins

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Clostridial ADP-ribosyltransferases ? Modification of low molecular weight GTP-binding proteins and of actin by clostridial toxins

Cited by 20 publications

References 92 publications

ADP‐ribosylation of actins by arginine‐specific ADP‐ribosyltransferase purified from chicken heterophils

ADP‐ribosylation of actins by arginine‐specific ADP‐ribosyltransferase purified from chicken heterophils

Disturbing Gtp-Binding Protein Function Through Microinjection Into The Visual Cell Of Limulus

Actin‐ADP‐Ribosylating Toxins: Cytotoxic Mechanisms ofClostridium botulinumC2 Toxin andClostridium perfringenslota Toxin

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