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J. Biol. Chem., Vol. 279, Issue 47, 49289-49297, November 19, 2004

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Characterization of Sea Urchin Transglutaminase, a Protein Regulated by Guanine/Adenine Nucleotides^*

Laura Zanetti, Filomena Ristoratore, Alessandra Bertoni, and Lucio Cariello

From the Biochemistry and Molecular Biology Laboratory, Stazione Zoologica Anton Dohrn, 80121 Napoli, Italy

Transglutaminases (TGs) are calcium-dependent enzymes that catalyze the transamidation of glutamine residues to form intermolecular isopeptide bonds. Nine distinct TGs have been identified in mammals, and three of them (types 2, 3, and 5) are regulated by GTP/ATP and are able to hydrolyze GTP, working as bifunctional enzymes. We have isolated a cDNA clone encoding a TG from a cDNA library prepared from the blastula stage of sea urchin Paracentrotus lividus (PlTG). The cDNA sequence has an open reading frame coding for a protein of 738 amino acids, including a Cys active site and two other residues critical for catalytic activity, His and Asp. We have studied its expression pattern by in situ hybridization and have also demonstrated that the in vitro expressed PlTG had GTP- and ATP-hydrolyzing activity; moreover, GTP inhibited the transamidating activity of this enzyme as it does that of human TG2, TG3, and TG5.

Received for publication, May 27, 2004 , and in revised form, September 17, 2004.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AJ439609.

^* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed. Tel.: 39-081-5833216; Fax: 39-081-7641355; E-mail: lcariel{at}szn.it.

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