Phytaspase Does Not Require Proteolytic Activity for Its Stress-Induced Internalization

Torosian, T.A.; Barsukova, A.I.; Chichkova, N.V.; Vartapetian, A.B.

Статья опубликована в высокорейтинговом журнале

Информация о цитировании статьи получена из Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 31 июля 2024 г.

Авторы: Torosian T.A., Barsukova A.I., Chichkova N.V., Vartapetian A.B.
Журнал: International Journal of Molecular Sciences
Том: 25
Год издания: 2024
Издательство: MDPI
Местоположение издательства: Basel, Switzerland
Номер статьи: 6729
DOI: 10.3390/ijms25126729
Аннотация: Phytaspases differ from other members of the plant subtilisin-like protease family by having rare aspartate cleavage specificity and unusual localization dynamics. Phytaspases aresecreted from healthy plant cells but are re-internalized upon perception of death-inducing stresses. Although proteolytic activity is required for the secretion of plant subtilases, its requirement for the retrograde transportation of phytaspases is currently unknown. To address this issue, we employed an approach to complement in trans the externalization of a prodomain-less form of Nicotiana tabacum phytaspase (NtPhyt) with the free prodomain in Nicotiana benthamiana leaf cells. Using this approach, the generation of the proteolytically active NtPhyt and its transport to the extracellular space at a level comparable to that of the native NtPhyt (synthesized as a canonical prodomain-containing precursor protein) were achieved. The application of this methodology to NtPhyt with a mutated catalytic Ser537 residue resulted in the secretion of the inactive, although processed (prodomain-free), protein as well. Notably, the externalized NtPhyt Ser537Ala mutant was still capable of retrograde transportation into plant cells upon the induction of oxidative stress. Our data thus indicate that the proteolytic activity of NtPhyt is dispensable for stress-induced retrograde transport of the enzyme.
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Phytaspase Does Not Require Proteolytic Activity for Its Stress-Induced Internalizationстатья

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