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Journal of Experimental Botany, Vol. 52, No. 361, pp. 1635-1645, August 1, 2001
© 2001 Oxford University Press


Original Papers

ß-Galactosidases with a lectin-like domain are expressed in strawberry1

Livio Trainotti, Riccardo Spinello, Anna Piovan, Silvia Spolaore and Giorgio Casadoro2

Dipartimento di Biologia, Università di Padova, Viale G. Colombo 3, I-35121 Padova, Italy

Strawberry fruits (Fragariaxananassa Duch.) undergo a marked softening during their ripening, and the process is accompanied by a release of free sugars with galactose among them. In this work total ß-galactosidase activity was measured in cell wall proteins from strawberry fruits at different developmental stages. Three full-length cDNAs (Faßgal1, Faßgal2 and Faßgal3, respectively) encoding different ß-galactosidases (EC 3.2.1.23) were isolated from a library representing red fruit transcripts. All of them could be detected both in fruits and in vegetative tissues. However, only Faßgal1 showed an increasing expression during the ripening stages up to a maximum in the red fruits, while the other two (Faßgal2 and Faßgal3) were mostly found in green fruits and became barely detectable during ripening proper. The three ß-galactosidase-encoding cDNAs were expressed in the yeast Pichia pastoris, and it was thus possible to demonstrate that each of them encode a ß-galactosidase. The expression of the three ß-galactosidase genes appears to be down-regulated by auxin, as already observed for other ripening-related genes of the non-climacteric strawberry. An unusual characteristic of two strawberry ß-galactosidases (Faßgal1 and Faßgal2) is that at the C-terminus of the enzymes a domain is found which is structurally related to known animal peptides with a sugar-binding ability.

Key words: Fruit ripening, ß-galactosidase, lectin-like domain, strawberry.


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