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Infection and Immunity, December 2001, p. 7663-7670, Vol. 69, No. 12
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.12.7663-7670.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Lysine and Polyamines Are Substrates for Transglutamination of Rho by the Bordetella Dermonecrotic Toxin

Gudula Schmidt,1,* Udo-Michael Goehring,1 Joerg Schirmer,1 Sandrine Uttenweiler-Joseph,2 Matthias Wilm,2 Mark Lohmann,3 Arnd Giese,1 Guenther Schmalzing,1 and Klaus Aktories1,*

Institut für Experimentelle und Klinische Pharmakologie und Toxikologie der Albert-Ludwigs-Universität Freiburg, D-79104 Freiburg,1 EMBL, D-69117 Heidelberg,2 and Biozentrum N260, Pharmakologisches Institut für Naturwissenschaftler, Johann Wolfgang Goethe-Universität, D-60439 Frankfurt,3 Germany

Received 25 June 2001/Returned for modification 7 August 2001/Accepted 5 September 2001

Bordetella dermonecrotic toxin (DNT) catalyzes the transglutamination of glutamine-63/61 of Rho GTPases, thereby constitutively activating Rho proteins. Here we identified second substrates for transglutamination of RhoA by DNT. The enzymatically active fragment of DNT (residues 1136 to 1451, Delta DNT) induced the incorporation of L-[14C]lysine in RhoA in a concentration-dependent manner. Also, Rac and Cdc42, but not Ras, were transglutaminated with lysine by Delta DNT. Transglutamination of the GTPase with L-lysine inhibited intrinsic and Rho-GAP-stimulated GTP hydrolysis of RhoA. In contrast to lysine, treatment of RhoA with alanine, arginine, and glutamine were not able to substitute for lysine in the transglutamination reaction. DNT increased the incorporation of L-[14C]lysine into embryonic bovine lung cells. Microinjection of GST-RhoA together with the enzymatically active DNT fragment into Xenopus oocytes, subsequent affinity purification of modified GST-RhoA, and mass spectrometry identified attachment of putrescine or spermidine at glutamine-63 of RhoA. A comparison of putrescine, spermidine, and lysine as substrates for DNT-induced transglutamination of RhoA revealed that lysine is a preferred second substrate at least in vitro.

* Corresponding author. Mailing address: Institut für Experimentelle und Klinische Pharmakologie und Toxikologie, Albert-Ludwigs-Universität Freiburg, Albert-Str. 25, D-79104 Freiburg, Germany. Phone: 49-761-203-5301. Fax: 49-761-203-5311. E-mail: aktories{at}uni-freiburg.de. E-mail: gudschmi{at}uni-freiburg.de.

Infection and Immunity, December 2001, p. 7663-7670, Vol. 69, No. 12
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.12.7663-7670.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Pop, M., Aktories, K., Schmidt, G. (2004). Isotype-specific Degradation of Rac Activated by the Cytotoxic Necrotizing Factor 1. J. Biol. Chem. 279: 35840-35848 [Abstract] [Full Text]  


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