Journal of Plant Research

, Volume 119, Issue 5, pp 469–478

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

  • Mauritz Venter
  • Jan-Hendrik Groenewald
  • Frederik C. Botha
Regular Paper

DOI: 10.1007/s10265-006-0009-4

Cite this article as:
Venter, M., Groenewald, JH. & Botha, F.C. J Plant Res (2006) 119: 469. doi:10.1007/s10265-006-0009-4


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.


Berry ripeningCold stressGrapevineV-PPase



Basic local alignment search tool


Eukaryotic linear motif


Expressed sequence tag


Long-range inverse PCR


Open reading frame


H+-transporting/vacuolar adenosine triphosphatase (EC


H+-translocating/vacuolar inorganic pyrophosphatase (EC

Copyright information

© The Botanical Society of Japan and Springer-Verlag 2006

Authors and Affiliations

  • Mauritz Venter
    • 1
  • Jan-Hendrik Groenewald
    • 1
  • Frederik C. Botha
    • 1
    • 2
  1. 1.Institute for Plant BiotechnologyStellenbosch UniversityMatielandSouth Africa
  2. 2.South African Sugarcane Research InstituteMount EdgecombeSouth Africa