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Molecular cloning of b-galactosidase from Japanese pear (Pyrus pyrifolia) and its gene expression with fruit ripening


Molecular cloning of b-galactosidase from Japanese pear (Pyrus pyrifolia) and its gene expression with fruit ripening



Plant and Cell Physiology 42(5): 2-8



ISSN/ISBN: 0032-0781

We have cloned a cDNA fragment encoding a b-galactosidase from Japanese pear (Pyrus pyrifolia) fruit (JP-GAL). It contained an untranslated sequence of 182 nucleotides at the 5' end, a presumptive coding sequence of 2,193 nucleotides and an untranslated sequence of 268 nucleotides including a polyadenylation signal and a poly (A) tail at the 3' end. It encoded a protein with a calculated molecular weight of 80.9 kDa which consists of 731 amino acids. Both the nucleotide and the deduced amino acid sequences showed a 98% sequence identity with that obtained from the apple b-galactosidase cDNA. The peptide sequence obtained from the purified Japanese pear b-galactosidase III matched the deduced amino acid sequence of SVSYDHKAIIINGQKRILISG (amino acid 25-45). Northern blot analysis showed that the probe derived from JP-GAL hybridized to a single 2.6 kb RNA. The mRNA was detected solely in the fruit; none was detected in the buds, leaves, roots or shoots of the Japanese pear. The steady-state level of the b-galactosidase mRNA was measured during fruit ripening in three cultivars, Housui, Kousui (early ripening) and Niitaka (late ripening). The results showed that regardless of the cultivar, no JP-GAL mRNA was detected in the immature fruit. Increment of the mRNA level with fruit ripening coincided with the increase in the b-galactosidase III activity. Our results showed that the expression of JP-GAL correlated with fruit softening and JP-GAL may be b-galactosidase III. Reprinted by permission of the publisher.

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Accession: 009913429

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