Compatible and self-incompatible pollination in Pyrus communis displays different polyamine levels and transglutaminase activity.
The polyamine (PA) content and the transglutaminase (TGase) activity have been investigated in Pyrus communis pollination with compatible and self-incompatible (SI) pollen in order to deepen their possible involvement in the progamic phase of plant reproduction. The PA distribution as free, perchloric acid (PCA)-soluble and PCA-insoluble fractions in ungerminated (UGP), germinating pollen (GP), styles and pollinated styles with compatible and SI pollens is discussed in the light of a possible role during pollination. Generally, the conjugated PAs both in PCA-soluble and PCA-insoluble fractions were higher than the free form. Within the conjugated PAs, the PCA-insoluble ones were the highest with the exception of the not pollinated styles. As TGase mediates some of the effects of PAs by covalently binding them to proteins, the activity of this enzyme, never checked before in styles and pollinated styles, was examined. In the SI styles, the TGase activity is higher in comparison to style-pollinated with compatible pollen, and high molecular mass cross-linked products were formed, suggesting an involvement of TGase in SI response. This is the first evidence on the presence of this enzyme activity in not pollinated and pollinated styles.
Del Duca
S
S
Dipartimento di Biologia e.s., Università degli Studi di Bologna, Via Irnerio 42, 40126 Bologna, Italy. stefano.delduca@unibo.it
Cai
G
G
Di Sandro
A
A
Serafini-Fracassini
D
D
D010940:Plant Proteins / Q000235:genetics / Q000378:metabolism*; D011058:Pollen / Q000201:enzymology / Q000235:genetics / Q000254:growth & development / Q000502:physiology; D054817:Pollination; D011073:Polyamines / Q000378:metabolism*; D031989:Pyrus / Q000201:enzymology / Q000235:genetics / Q000254:growth & development / Q000502:physiology*; D011503:Transglutaminases / Q000235:genetics / Q000378:metabolism*
D010940:Plant Proteins; D011073:Polyamines; D011503:Transglutaminases