Transglutaminases have been studied in plants since twenty years in investigations aimed at interpreting the molecular mechanisms by which polyamines affect plant growth and differentiation. The post-translational modification of proteins by polyamines forming inter- or intra-molecular cross-links has been the main transglutaminase reaction studied in plants. Transglutaminase activity is ubiquitous: it has been detected in different organs and sub-cellular compartments, chloroplasts being the best-studied organelles. Specificity and similarity with animal transglutaminases are discussed in the light of their biochemical characteristics and functional roles. Possible roles concern the structural modification of specific proteins. They modify actin and tubulin, also influencing motor proteins, thus exerting a role on cell growth and cell structure. In chloroplasts, transglutaminases appear to stabilise the photosynthetic complexes and Rubisco, being regulated by light and other factors, and possibly exerting a positive effect on photosynthesis and photoprotection. Preliminary reports suggest an involvement in construction/organisation of the cell wall and extracellular matrix in relationship with fertilisation. Other roles appear to be related to stresses, senescence and programmed cell death. The cross recognition of substrates between plant and animal enzymes suggest both similarities and differences. The few plant transglutaminases sequenced so far have little sequence homology with the best-known animal enzymes, except for the catalytic triad; however, they share a possible structural homology. Proofs of their catalytic activity are: 1. their ability to produce glutamyl-polyamine derivatives, 2. their recognition by animal transglutaminase antibodies, 3. biochemical features such as calcium- and GTP-dependency, etc. 4. Inhibition by specific inhibitors of animal transglutaminases. However, many of their fundamental physiological properties still remain elusive. At present, it is not possible to classify this enzyme family in plants owing to the scarcity of information on genes encoding them. FUNDING: MUR -Progetti di Rilevante Interesse Nazionale, - Interaction mechanisms for protein mediators of flower incompatibility in fertilisation of fruit trees, to D. S-F. “Crossallergenicity”, Progetto Strategico d’Ateneo E.F. 2006, Università di Bologna.

Transglutaminases, aspects of their enzymatic activities in plants and animals.

SERAFINI FRACASSINI, DONATELLA;DELLA MEA, MASSIMILIANO;IORIO, ROSA ANNA;DEL DUCA, STEFANO
2008

Abstract

Transglutaminases have been studied in plants since twenty years in investigations aimed at interpreting the molecular mechanisms by which polyamines affect plant growth and differentiation. The post-translational modification of proteins by polyamines forming inter- or intra-molecular cross-links has been the main transglutaminase reaction studied in plants. Transglutaminase activity is ubiquitous: it has been detected in different organs and sub-cellular compartments, chloroplasts being the best-studied organelles. Specificity and similarity with animal transglutaminases are discussed in the light of their biochemical characteristics and functional roles. Possible roles concern the structural modification of specific proteins. They modify actin and tubulin, also influencing motor proteins, thus exerting a role on cell growth and cell structure. In chloroplasts, transglutaminases appear to stabilise the photosynthetic complexes and Rubisco, being regulated by light and other factors, and possibly exerting a positive effect on photosynthesis and photoprotection. Preliminary reports suggest an involvement in construction/organisation of the cell wall and extracellular matrix in relationship with fertilisation. Other roles appear to be related to stresses, senescence and programmed cell death. The cross recognition of substrates between plant and animal enzymes suggest both similarities and differences. The few plant transglutaminases sequenced so far have little sequence homology with the best-known animal enzymes, except for the catalytic triad; however, they share a possible structural homology. Proofs of their catalytic activity are: 1. their ability to produce glutamyl-polyamine derivatives, 2. their recognition by animal transglutaminase antibodies, 3. biochemical features such as calcium- and GTP-dependency, etc. 4. Inhibition by specific inhibitors of animal transglutaminases. However, many of their fundamental physiological properties still remain elusive. At present, it is not possible to classify this enzyme family in plants owing to the scarcity of information on genes encoding them. FUNDING: MUR -Progetti di Rilevante Interesse Nazionale, - Interaction mechanisms for protein mediators of flower incompatibility in fertilisation of fruit trees, to D. S-F. “Crossallergenicity”, Progetto Strategico d’Ateneo E.F. 2006, Università di Bologna.
2008
54° Convegno GEI Gruppo Embriologico Italiano
37
37
SERAFINI-FRACASSINI D.;| DELLA MEA M.|; IORIO R; DEL DUCA S;
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11585/87583
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