Characterization of Solanum tuberosum multicystatin and the significance of core domains

The Plant Cell
Abigail R GreenChulhee Kang

Abstract

Potato (Solanum tuberosum) multicystatin (PMC) is a unique cystatin composed of eight repeating units, each capable of inhibiting cysteine proteases. PMC is a composite of several cystatins linked by trypsin-sensitive (serine protease) domains and undergoes transitions between soluble and crystalline forms. However, the significance and the regulatory mechanism or mechanisms governing these transitions are not clearly established. Here, we report the 2.2-Å crystal structure of the trypsin-resistant PMC core consisting of the fifth, sixth, and seventh domains. The observed interdomain interaction explains PMC's resistance to trypsin and pH-dependent solubility/aggregation. Under acidic pH, weakening of the interdomain interactions exposes individual domains, resulting in not only depolymerization of the crystalline form but also exposure of cystatin domains for inhibition of cysteine proteases. This in turn allows serine protease-mediated fragmentation of PMC, producing ∼ 10-kD domains with intact inhibitory capacity and faster diffusion, thus enhancing PMC's inhibitory ability toward cysteine proteases. The crystal structure, light-scattering experiments, isothermal titration calorimetry, and site-directed mutagenesis confirmed...Continue Reading

Citations

Jan 23, 2016·The New Phytologist·Friederike M Grosse-Holz, Renier A L van der Hoorn
Feb 16, 2016·Biochemistry. Biokhimii︠a︡·A A Zamyatnin
Aug 13, 2015·Insect Biochemistry and Molecular Biology·Juan VorsterDominique Michaud
Oct 25, 2016·International Journal of Molecular Sciences·Manuel MartinezIsabel Diaz
Nov 16, 2016·Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire·Shumaila KhanBilqees Bano

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