Molecular Genetics and Genomics

, Volume 287, Issue 6, pp 451–460 | Cite as

Allele diversity for the apoplastic invertase inhibitor gene from potato

  • Sagar S. Datir
  • Julie M. Latimer
  • Susan J. Thomson
  • Hayley J. Ridgway
  • Anthony J. Conner
  • Jeanne M. E. JacobsEmail author
Original Paper


In planta the enzymatic activity of apoplastic and vacuolar invertases is controlled by inhibitory proteins. Although these invertase inhibitors (apoplastic and vacuolar forms) have been implicated as contributing to resistance to cold-induced sweetening (CIS) in tubers of potato (Solanum tuberosum L.), there is a lack of information on the structure and allelic diversity of the apoplastic invertase inhibitor genes. We have PCR-isolated and sequenced the alleles of the apoplastic invertase inhibitor gene (Stinh1) from three tetraploid potato genotypes: 1021/1 (a genotype with very high tolerance to CIS), ‘Karaka’ and ‘Summer Delight’ (two cultivars that are highly susceptible to CIS). In total, five alleles were identified in these genotypes, of which four (Stinh1-c, Stinh1-d, Stinh1-e, Stinh1-f) were novel. An analysis of allele diversity was conducted by incorporating previously published sequences of apoplastic invertase inhibitors from potato. Eight alleles were assessed for sequence polymorphism in the two exons and the single hypervariable intron. Contrary to the hypervariable intron, only 65 single nucleotide polymorphisms were observed in the exons, of which 42 confer amino acid substitutions. Phylogenetic analysis of amino acid sequences indicates that the alleles of the invertase inhibitor are highly conserved amongst members of the Solanaceae family.


Solanum tuberosum Cold-induced sweetening Stinh1 Sequence polymorphism Allelic variation 



We would like to thank Russell Genet for supplying potato tubers, Samantha Baldwin for help in primer design, and Mei Meiyalaghan and Mark Fiers for stimulating discussions. This work was supported by Ministry of Science & Innovation (New Zealand) contract C02X0805 to The New Zealand Institute for Plant & Food Research Limited, New Zealand, and grants from Lincoln University, New Zealand (SSD) and a New Zealand International Doctoral Research Scholarship (SSD).

Supplementary material

438_2012_690_MOESM1_ESM.pdf (214 kb)
Supplementary material 1 (PDF 216 kb)
438_2012_690_MOESM2_ESM.pdf (89 kb)
Supplementary material 2 (PDF 92 kb)


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Copyright information

© Springer-Verlag 2012

Authors and Affiliations

  • Sagar S. Datir
    • 1
    • 2
  • Julie M. Latimer
    • 1
  • Susan J. Thomson
    • 1
  • Hayley J. Ridgway
    • 2
  • Anthony J. Conner
    • 1
    • 2
  • Jeanne M. E. Jacobs
    • 1
    Email author
  1. 1.The New Zealand Institute for Plant & Food Research LimitedChristchurchNew Zealand
  2. 2.Faculty of Agriculture and Life SciencesLincoln UniversityCanterburyNew Zealand

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