Interaction proteins of invertase and invertase inhibitor in cold-stored potato tubers suggested a protein complex underlying post-translational regulation of invertase
Abstract
The activity of vacuolar invertase (VI) is vital to potato cold-induced sweetening (CIS). A post-translational regulation of VI activity has been proposed which involves invertase inhibitor (VIH), but the mechanism for the interaction between VI and VIH has not been fully understood. To identify the potential partners of VI and VIH, two cDNA libraries were respectively constructed from CIS-resistant wild potato species Solanum berthaultii and CIS-sensitive potato cultivar AC035-01 for the yeast two-hybrid analysis. The StvacINV1 (one of the potato VIs) and StInvInh2B (one of the potato VIHs), previously identified to be associated with potato CIS, were used as baits to screen the two libraries. Through positive selection and sequencing, 27 potential target proteins of StvacINV1 and eight of StInvInh2B were clarified. The Kunitz-type protein inhibitors were captured by StvacINV1 in both libraries and the interaction between them was confirmed by bimolecular fluorescence complementation assay in tobacco cells, reinforcing a fundamental interaction between VI and VIH. Notably, a sucrose non-fermenting-1-related protein kinase 1 was captured by both the baits, suggesting that a protein complex could be necessary for fine turning of the invertase activity. The target proteins clarified in present research provide a route to elucidate the mechanism by which the VI activity can be subtly modulated.
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INVinh has been reported to mediate the post-translational regulation of invertase, and the activity of one invertase might be regulated by several INVinhs.
“However, INVinh has been reported to mediate the post-translational regulation of invertase, and the activity of one invertase might be regulated by several INVinhs (Link et al., 2004; Lin et al., 2013).”
From Comparative Transcriptome Analysis Reveals Critical Function of Sucrose Metabolism Related-Enzymes in Starch Accumulation in the Storage Root of Sweet Potato (2017) · cites this paper as Lin et al., 2013
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- Authors
- Lin, Y., Liu, J., Liu, X., Ou, Y., Li, M., Zhang, H., Song, B., & Xie, C.
- Affiliations
- Huazhong Agricultural University (CN)
- Corresponding author
- Song, Botao
- Xie, Conghua
- Venue
- Plant Physiology and Biochemistry
- Publisher
- Elsevier BV
- Published
- 2013-12
- Volume
- 73
- Pages
- 237-244
- ISSN
- 0981-9428 (ISSN-L)
- OpenAlex
- W2040781054
- Cited by
- 24
- References
- 40
- Citations by year
- 2025: 1 · 2024: 1 · 2023: 1 · 2021: 1 · 2020: 9 · 2019: 2 · 2018: 1 · 2017: 3 · 2015: 1 · 2014: 3 · 2013: 1
- FWCI
- 2.01
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Plant Physiology and Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Science Foundation of China (30800754, 31201258)
- Chenguang Project of Wuhan City (201050231068)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Postharvest Quality and Shelf Life Management
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant nutrient uptake and metabolism
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Molecular Biology Research
- Keywords
- vacuolar invertase, invertase inhibitor, post-translational regulation, protein-protein interaction, protein complexes, Solanum berthaultii, cold storage, potato tubers
- MeSH terms
- Diet, Enzyme Inhibitors, Plant Proteins, Solanum tuberosum, Protein Kinases, Protein Processing, Post-Translational, Species Specificity, Sucrose, Taste, Nicotiana, Vacuoles, Cryopreservation, Genes, Plant, DNA, Complementary, Gene Expression Regulation, Plant, Plant Tubers, beta-Fructofuranosidase, Food Storage
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