Distinct patterns of activation of papain-like cysteine protease Triticain-alpha in vivoстатьяТезисы
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Дата последнего поиска статьи во внешних источниках: 22 февраля 2019 г.
Аннотация:Papainlike cysteine proteases (PLCPs) in plants and animals participate in numerous physiological processes. They are synthesized as preproenzymes consisting of Nterminal signal peptide, inhibitory prodomain and proteolytic domain. The proenzyme activation occurs through autocatalytic mechanism implying intra or intermolecular hydrolysis of prodomain or by other proteases acting upstream in the proteolytic cascade. PLCPs commonly localize in lysosomes or vacuolesbeing activated and stable at low pH levels. Despite recent progress in studying of PLCPs, there is a lack of knowledge concerning in vivo properties of these proteases, for most of which the enzymatic cascades, subcellular localization, and specific substrates remain unknown. Triticaina is a PLCP from Triticum aestivum L, which was detected in wheat seedlings. Previously, we have cloned Triticaina, identified domain structure of the enzyme necessary for its maturation and demonstrated its glutenase and collagenase activities. We also developed a cheap and efficient protocol for producing the active recombinant enzyme. In this study, using nonaqueous fractionation method we have demonstrated for the first time that the mature endogenous Triticaina is specifically accumulated in vacuoles of T. aestivum L leaves, whereas the fulllength protein and its low MW variants are localized to nonvacuolar fractions. MS analysis of Triticaina fragments allowed us to identify sites of the enzyme proteolysis specific to vacuolar and nonvacuolar fractions. Based on this data, we suggest that autocatalytic maturation of Triticaina is characteristic of vacuoles, whereas outside these compartments the maturation is held by other intracellular proteases. Since homolog of Triticaina was shown to be a substrate of metacaspases involved in cell death of xylem elements, we suggest a possible association of Triticaina with this process as well. This work was funded by the Russian Science Foundation (grant #161510410).