<i>Arabidopsis thaliana</i> Phytocystatin 6 Forms Functional Oligomer and Amyloid Fibril States.

ABSTRACT: Cystatins encode a high functional variability not only because of their ability to inhibit different classes of proteases but also because of their propensity to form oligomers and amyloid fibrils. Phytocystatins, essential regulators of protease activity in plants, specifically inhibit papain-like cysteine proteases (PLCPs) and legumains through two distinct cystatin domains. Mammalian cystatins can form amyloid fibrils; however, the potential for amyloid fibril formation of phytocystatins remains unknown. In this study, we demonstrate that Arabidopsis thaliana phytocystatin 6 (AtCYT6) exists as a mixture of monomeric, dimeric, and oligomeric forms in solution. Noncovalent oligomerization was facilitated by the N-terminal cystatin domain, while covalent dimerization occurred throu

SUBMITTER: Santos NP 

PROVIDER: S-EPMC10702442 | biostudies-literature | 2023 Dec

REPOSITORIES: biostudies-literature