ArticleJournal of experimental botany2016
RhVI1 is a membrane-anchored vacuolar invertase highly expressed in Rosa hybrida L. petals.
Article in Journal of experimental botany, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 13 citations in OpenAlex.
- Involvement of NtInvVR1 in the increase of reducing sugars during the curing of virginia tobacco.Scientific reports · 2026Article
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- Abscisic Acid Regulates Carbohydrate Metabolism, Redox Homeostasis and Hormonal Regulation to Enhance Cold Tolerance in Spring Barley.International journal of molecular sciences · 2023Article
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- The Role of Iron and Copper on the Oligomerization Dynamics of DR_2577, the Main S-Layer Protein ofFrontiers in microbiology · 2019Article
- iTRAQ-based quantitative proteomic analysis reveals dynamic changes during daylily flower senescence.Planta · 2018Article
- New insights into the operative network of FaEO, an enone oxidoreductase from Fragaria x ananassa Duch.Plant molecular biology · 2017Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Invertases are a widespread group of enzymes that catalyse the conversion of sucrose into fructose and glucose. Plants invertases and their substrates are essential factors that play an active role in primary metabolism and in cellular differentiation and by these activities they sustain development and growth. Being naturally present in multiple isoforms, invertases are known to be highly differentiated and tissue specific in such a way that every isoform is characteristic of a specific part of the plant. In this work, we report the identification of the invertase RhVI1 that was found to be highly expressed in rose petals. A characterization of this protein revealed that RhVI1 is a glycosylated membrane-anchored protein associated with the cytosolic side of the vacuolar membrane which occurs in vivo in a monomeric form. Purification yields have shown that the levels of expression decreased during the passage of petals from buds to mature and pre-senescent flowers. Moreover, the activity assay indicates RhVI1 to be an acidic vacuolar invertase. The physiological implications of these findings are discussed, suggesting a possible role of this protein during anthesis.
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