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Plant and animal transglutaminases: do similar functions imply similar structures?

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Abstract

In plants the post-translational modification of proteins by polyamines catalysed by transglutaminases has been studied since 1987; it was identified by the production of glutamyl-polyamine derivatives, biochemical features, recognition by animal antibodies and modification of typical animal substrates. Transglutaminases are widespread in all plant organs and cell compartments studied until now, chloroplast being the most studied. Substrates are: photosynthetic complexes and Rubisco in chloroplasts, cytoskeleton and cell wall proteins. Roles either specific of plants or in common with animals are related to photosynthesis, fertilisation, stresses, senescence and programmed cell death, showing that the catalytic function is conserved across the kingdoms. AtPng1p, the first plant transglutaminase sequenced shows undetectable sequence homology to the animal enzymes, except for the catalytic triad. It is, however, endowed with a calcium-dependent activity that allowed us to build a three-dimensional model adopting as a template the animal tranglutaminase 2.

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Acknowledgments

Funding: The financial support of our recent research by the Ministero dell’Università e della Ricerca Scientifica e Tecnologica (FIRB Project No. RBAU01KZ49- Proteine modificate post-traduzionalmente da transglutaminasi durante la morte cellulare programata; PRIN Project of 2005–2007- Interaction mechanisms for protein mediators of flower incompatibility in fertilization of fruit trees, to D.S-F) and Bologna University (Cross allergens in pollen and fruits: modulation by climate changes of their allergenic potential, Progetto Strategico di Ateneo 2006 to D.S-F) are gratefully acknowledged. RC acknowledges the receipt of the following grants: FIRB 2003 LIBI-International Laboratory of Bioinformatics and the support to the Bologna node of the Biosapiens Network of Excellence project within the European Union’s VI Framework Programme (contract number LSGH-CT-2003-503265). We thank Mr. N. Mele for the technical assistance in figure preparation.

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  1. Unit of Plant Cell Growth and Differentiation, Dipartimento di Biologia Evoluzionistica Sperimentale, Sede Botanica, University of Bologna, via Irnerio 42, 40126, Bologna, Italy

    Donatella Serafini-Fracassini, Massimiliano Della Mea & Stefano Del Duca

  2. Biocomputing Group, CIRB/CIG-Interdipartimental Centers for Researches, Dipartimento di Biologia Evoluzionistica Sperimentale, University of Bologna, via San Giacomo 9/2, 40126, Bologna, Italy

    Gianluca Tasco & Rita Casadio

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  1. Donatella Serafini-Fracassini
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  2. Massimiliano Della Mea
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Correspondence to Donatella Serafini-Fracassini.

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Serafini-Fracassini, D., Della Mea, M., Tasco, G. et al. Plant and animal transglutaminases: do similar functions imply similar structures?. Amino Acids 36, 643–657 (2009). https://doi.org/10.1007/s00726-008-0131-9

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