ArticleJournal of bacteriology2000
Characterization of the enzymatic component of Clostridium perfringens iota-toxin.
Article in Journal of bacteriology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 51 citations in OpenAlex.
- Article
- Structure of the cell-binding component of theProceedings of the National Academy of Sciences of the United States of America · 2020Article
- ParST is a widespread toxin-antitoxin module that targets nucleotide metabolism.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Crystal structure and structure-based mutagenesis of actin-specific ADP-ribosylating toxin CPILE-a as novel enterotoxin.PloS one · 2017Article
- Article
- Functional significance of active site residues in the enzymatic component of theBiochemistry and biophysics reports · 2016Article
- Roles of Asp179 and Glu270 in ADP-Ribosylation of Actin by Clostridium perfringens Iota Toxin.PloS one · 2015Article
- Clostridium and bacillus binary enterotoxins: bad for the bowels, and eukaryotic being.Toxins · 2014Review
- BEC, a novel enterotoxin of Clostridium perfringens found in human clinical isolates from acute gastroenteritis outbreaks.Infection and immunity · 2014Article
- High-resolution crystal structure of Streptococcus pyogenes β-NAD⁺ glycohydrolase in complex with its endogenous inhibitor IFS reveals a highly water-rich interface.Journal of synchrotron radiation · 2013Article
- Intracellular trafficking of Clostridium perfringens iota-toxin b.Infection and immunity · 2012Article
- Molecular and biological characterization of Streptococcal SpyA-mediated ADP-ribosylation of intermediate filament protein vimentin.The Journal of biological chemistry · 2012Article
- Disruption of SCO5461 gene coding for a mono-ADP-ribosyltransferase enzyme produces a conditional pleiotropic phenotype affecting morphological differentiation and antibiotic production in Streptomyces coelicolor.Journal of microbiology (Seoul, Korea) · 2012Article
- Cholera- and anthrax-like toxins are among several new ADP-ribosyltransferases.PLoS computational biology · 2010Article
- The long-lived nature of clostridium perfringens iota toxin in mammalian cells induces delayed apoptosis.Infection and immunity · 2009Article
- Article
- Structural basis for substrate recognition in the enzymatic component of ADP-ribosyltransferase toxin CDTa from Clostridium difficile.The Journal of biological chemistry · 2009Article
- Structural basis of actin recognition and arginine ADP-ribosylation by Clostridium perfringens iota-toxin.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Binary bacterial toxins: biochemistry, biology, and applications of common Clostridium and Bacillus proteins.Microbiology and molecular biology reviews : MMBR · 2004Review
- Binding and internalization of Clostridium perfringens iota-toxin in lipid rafts.Infection and immunity · 2004Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The iota(a) component (i(a)) of Clostridium perfringens ADP ribosylates nonmuscle beta/gamma actin and skeletal muscle alpha-actin. Replacement of Arg-295 in i(a) with alanine led to a complete loss of NAD(+)-glycohydrolase (NADase) and ADP-ribosyltransferase (ARTase); that of the residue with lysine caused a drastic reduction in NADase and ARTase activities (<0.1% of the wild-type activities) but did not completely diminish them. Substitution of alanine for Glu-378 and Glu-380 caused a complete loss of NADase and ARTase. However, exchange of Glu-378 to aspartic acid or glutamine resulted in little effect on NADase activity but a drastic reduction in ARTase activity (<0.1% of the wild-type activity). Exchange of Glu-380 to aspartic acid caused a drastic reduction in NADase and ARTase activities (<0.1% of the wild-type activities) but did not completely diminish them; that of the residue to glutamine caused a complete loss of ARTase activity. Replacement of Ser-338 with alanine resulted in 0.7 to 2.3% wild-type activities, and that of Ser-340 and Thr-339 caused a reduction in these activities of 5 to 30% wild-type activities. The kinetic analysis showed that Arg-295 and Ser-338 also play an important role in the binding of NAD(+) to i(a), that Arg-295, Glu-380, and Ser-338 play a crucial role in the catalytic rate of NADase activity, and that these three amino acid residues and Glu-378 are essential for ARTase activity. The effect of amino acid replacement in i(a) on ARTase activity was similar to that on lethal and cytotoxic activities, suggesting that lethal and cytotoxic activities in i(a) are dependent on ARTase activity.
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