ArticleBotanical studies2014
Functional characterization of the N-terminal and C-terminal domains of a sesame group II phytocystatin.
Article in Botanical studies, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 10 citations in OpenAlex.
- Differential response of silencing HvIcy2 barley plants against Magnaporthe oryzae infection and light deprivation.BMC plant biology · 2018Article
- The wheat multidomain cystatin TaMDC1 displays antifungal, antibacterial, and insecticidal activities in planta.Plant cell reports · 2018Article
- Rice bifunctional phytocystatin is a dual modulator of legumain and papain-like proteases.Plant molecular biology · 2016Article
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4 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
backgroundPhytocystatins are natural inhibitors of cysteine protease, and may regulate endo- or exo-genous proteolytic activities in plants. They are classified into Group I and II differing by the presence of C-terminal extension of Group II. A cDNA fragment encoding a Group II phytosystatin, SiCYS was previously obtained from sesame seeds.
resultsSiCYS as well as its two structural domains, N-terminal and C-terminal domains (SiCYS-N and SiCYS-C), was expressed in Escherichia coli. The recombinant SiCYS and SiCYS-N showed inhibitory activity against papain. The K i values of SiCYS and SiCYS-N were ~1.9 ×10
conclusionSiCYS exhibited more effective papain-inhibitory activity than SiCYS-N; while SiCYS-C had almost no inhibitory activity. All displayed similar antifungal activities indicating that there is no correlation between antifungal and papain-inhibitory activities. Structural and sequence analyses suggest that the C-terminal domain of SiCYS may be originated from gene duplication to enhance its inhibitory activity.
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