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J Plant Res. 2006 Sep;119(5):469-78. Epub 2006 Aug 19.

Sequence analysis and transcriptional profiling of two vacuolar H+ -pyrophosphatase isoforms in Vitis vinifera.

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Institute for Plant Biotechnology, Stellenbosch University, Private Bag X1, Matieland, South Africa.


Gene expression of grapevine vacuolar H(+)-pyrophosphatase (V-PPase EC during fruit ripening has previously been reported. Here we report on putative multiple V-PPase isoforms in grapevine. In this study a full-length cDNA sequence with an open reading frame of 2,295 nucleotides encoding a V-PPase gene (vpp2: acc. nr. AJ557256) was cloned. Sequence analyses of the deduced amino acid residues and RT-PCR experiments indicated that Vitis vinifera L. has at least two distinct isoforms of the V-PPase gene. Bioinformatic analyses of 13 V-PPase protein sequences revealed two highly conserved motifs associated with pyrophosphate (PPi) binding and response to stress, respectively. Both V-PPase isoforms were expressed at higher levels in the late post-véraison stage of grape berry ripening. Results also showed that the expression of grapevine V-PPase was induced by cold stress.

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