Characterization of the enzymatic activity of Clostridium perfringens TpeL.

Toxicon

Institut Pasteur, Unité des Bactéries anaérobies et Toxines, 25 rue du Dr Roux, 75724 Paris Cedex 15, France.

Published: December 2013

AI Article Synopsis

  • TpeL is a toxin from Clostridium perfringens that modifies Ras proteins using specific sugars as cosubstrates.
  • The research shows that TpeL primarily glucosaminates three types of Ras (cH-Ras, N-Ras, K-Ras) and does so less with Rap1a and R-Ras3, while having little effect on Rac1.
  • Unlike previous studies, this study confirms that Ral is not affected by TpeL and identifies that cH-Ras is modified at the specific site Thr35.

Article Abstract

TpeL is a toxin produced by Clostridium perfringens which belongs to the large clostridial glucosylating toxin family. It was shown that TpeL modifies Ras using UDP-glucose or UDP-N-acetylglucosamine as cosubstrates (Guttenberg et al., 2012; Nagahama et al., 2011). We confirmed that TpeL preferentially glucosaminates the three isoforms of Ras (cH-Ras, N-Ras, and K-Ras) from UDP-N-acetylglucosamine and to a lower extent Rap1a and R-Ras3, and very weakly Rac1. In contrast to previous report, we observed that Ral was not a substrate of TpeL. In addition, we confirmed by in vitro glucosylation and mass spectrometry that TpeL modifies cH-Ras at Thr35.

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Source
http://dx.doi.org/10.1016/j.toxicon.2013.07.003DOI Listing

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