The pear self-incompatibility in the cv Abbé Fètel (P. communis) has been investigated in order to identify the S-alleles and pollen putative determinant transglutaminase (TGase), an enzyme able to post-translationally forming bridges among proteins. In the self-pollinated style (incompatible system), the activity of TGase is stimulated in comparison to style-pollinated with compatible pollen (compatible system), and high molecular mass cross-linked products are formed. High mass aggregates of tubulin, and punctuate aggregates of actin were observed in the incompatible system, suggesting a role of cytoskeleton in SI. In vitro experiments with purified pollen TGase and purified actin and tubulin, also incubated with kinesin and myosin motor-proteins, show that the inhibition of tube growth in incompatible crossing might be mediated by a cytoskeleton abnormal reorganisation caused by cross-linked protein networks catalysed by TGase. A molecular approach to clone pear TGase and S-RNases has been performed. The high homology between the pear and apple TGase sequences suggests that the good knowledge of the apple isoform can be transferred to pear. Contrarily to the pollen determinant, S- RNases have been very well characterised in pear and several S-alleles were identified. The authors have also approached the possible key role carried out by TGase in controlling the interaction between stylar RNases and pollen determinants of the SI mechanism. The update characterization of the European pear S-allele variability allows to set the pear interfertility groups.

Pollen Transglutaminase Characterization and S-Allele Segregation in Pear Self Incompatibility (Pyrus communis).

DI SANDRO, ALESSIA;SERAFINI FRACASSINI, DONATELLA;DEL DUCA, STEFANO;DE FRANCESCHI, PAOLO;DONDINI, LUCA;TASSINARI, PAOLA;SANSAVINI, SILVIERO;
2007

Abstract

The pear self-incompatibility in the cv Abbé Fètel (P. communis) has been investigated in order to identify the S-alleles and pollen putative determinant transglutaminase (TGase), an enzyme able to post-translationally forming bridges among proteins. In the self-pollinated style (incompatible system), the activity of TGase is stimulated in comparison to style-pollinated with compatible pollen (compatible system), and high molecular mass cross-linked products are formed. High mass aggregates of tubulin, and punctuate aggregates of actin were observed in the incompatible system, suggesting a role of cytoskeleton in SI. In vitro experiments with purified pollen TGase and purified actin and tubulin, also incubated with kinesin and myosin motor-proteins, show that the inhibition of tube growth in incompatible crossing might be mediated by a cytoskeleton abnormal reorganisation caused by cross-linked protein networks catalysed by TGase. A molecular approach to clone pear TGase and S-RNases has been performed. The high homology between the pear and apple TGase sequences suggests that the good knowledge of the apple isoform can be transferred to pear. Contrarily to the pollen determinant, S- RNases have been very well characterised in pear and several S-alleles were identified. The authors have also approached the possible key role carried out by TGase in controlling the interaction between stylar RNases and pollen determinants of the SI mechanism. The update characterization of the European pear S-allele variability allows to set the pear interfertility groups.
10th International Pear Symposium. Programme and Abstract.
42
42
Di Sandro A; Serafini-Fracassini D.; Del Duca S. ; De Franceschi P.; Dondini L.; Tassinari P.; Sansavini S.; Faleri C.; G Cai.
File in questo prodotto:
Eventuali allegati, non sono esposti

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11585/57420
 Attenzione

Attenzione! I dati visualizzati non sono stati sottoposti a validazione da parte dell'ateneo

Citazioni
  • ???jsp.display-item.citation.pmc??? ND
  • Scopus ND
  • ???jsp.display-item.citation.isi??? ND
social impact