Plant proteases: from molecular mechanisms to functions in development and immunity

Hoorn, Renier A. L. van der; Klemenčič, Marina

doi:10.1093/jxb/erab129

Cited by 22 publications

(23 citation statements)

References 12 publications

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“…Proteolysis, engaging a broad spectrum of hydrolytic enzymes called proteases (peptidases), is one of the most important biochemical processes required for protein metabolism of all living organisms [1]. In plants, these enzymes participate in many key physiological processes under both normal and stressful environmental conditions [2]. For example, during seed germination, proteases carry out degradation of storage proteins to provide the growing plants with nitrogen in the form of free amino acids and inorganic nitrogen compounds [3].…”

Section: Introductionmentioning

confidence: 99%

Proteolytic and Structural Changes in Rye and Triticale Roots under Aluminum Stress

Szewińska

Różańska

Papierowska

et al. 2021

Cells

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Proteolysis and structural adjustments are significant for defense against heavy metals. The purpose of this study was to evaluate whether the Al3+ stress alters protease activity and the anatomy of cereale roots. Azocaseinolytic and gelatinolytic measurements, transcript-level analysis of phytocystatins, and observations under microscopes were performed on the roots of Al3+-tolerant rye and tolerant and sensitive triticales exposed to Al3+. In rye and triticales, the azocaseinolytic activity was higher in treated roots. The gelatinolytic activity in the roots of rye was enhanced between 12 and 24 h in treated roots, and decreased at 48 h. The gelatinolytic activity in treated roots of tolerant triticale was the highest at 24 h and the lowest at 12 h, whereas in treated roots of sensitive triticale it was lowest at 12 h but was enhanced at 24 and 48 h. These changes were accompanied by increased transcript levels of phytocystatins in rye and triticale-treated roots. Light microscope analysis of rye roots revealed disintegration of rhizodermis in treated roots at 48 h and indicated the involvement of root border cells in rye defense against Al3+. The ultrastructural analysis showed vacuoles containing electron-dense precipitates. We postulate that proteolytic-antiproteolytic balance and structural acclimation reinforce the fine-tuning to Al3+.

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Section: Introductionmentioning

confidence: 99%

Proteolytic and Structural Changes in Rye and Triticale Roots under Aluminum Stress

Szewińska

Różańska

Papierowska

et al. 2021

Cells

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“…In 25 LLDR proteins with no linusorbs identi ed, these sites may be also recognized by the same family of protease, but the particular protease homologue may function differently from catalyzing linusorb synthesis. Proteases have been shown to exhibit various functions in almost all aspects of plant life, including development, homeostasis, stress response and defense [45].…”

Section: Pro Le-based Mining Is Suitable For Diversity Of Orbitide-re...mentioning

confidence: 99%

The flax genome reveals orbitide diversity

Song

Burbridge

Sharbel

et al. 2022

Preprint

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Background: Ribosomally-synthesized cyclic peptides are widely found in plants and show useful bioactivities for humans. The identification of cyclic peptide sequences and their precursor proteins is facilitated by the growing number of sequenced genomes. While previous research largely focused on the chemical diversity of these peptides across various species, there is little attention to a broader range of potential peptides that are not chemically identified. Results: A pioneering study was initiated to explore the genetic diversity of linusorbs, a group of cyclic peptides uniquely occurring in cultivated flax (Linum usitatissimum). Phylogenetic analysis categorized the 5 known linusorb precursor proteins into two clades and one singleton. Preliminary tBLASTn search of the published flax genome using the whole protein sequence as query could only retrieve its homologues within the same clade. This limitation was overcome using a profile-based mining strategy. After genome reannotation, a hidden Markov Model (HMM)-based approach identified 58 repeats homologous to the linusorb-embedded repeats in 8 novel proteins, meaning that they likely share common ancestry with the linusorb-embedded repeats. Subsequently, we developed a customized profile composed of a random linusorb-like domain (LLD) flanked by 5 conserved sites and used it for string search of the proteome, which extracted 281 LLD-containing repeats (LLDRs) in 25 proteins. Comparative analysis of different repeat categories suggested that the 5 conserved flanking sites among the non-homologous repeats have undergone convergent evolution driven by functional selection. Conclusions: The profile-based mining approach is suitable for analyzing repetitive sequences. The 25 LLDR proteins identified herein represent the potential diversity of cyclic peptides within the flax genome and lay a foundation for further studies on the functions and evolution of these protein tandem repeats.

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“…Some exceptions are Ara12 from A. thaliana, RSIP from maize, and C1 from soybean, showing an optimum pH between 3.5 and 6.5. [9] Furthermore, diisopropyl-fluorophosphate and phenylmethylsulfonyl fluoride are serine peptidase inhibitors.…”

Section: Introductionmentioning

confidence: 99%

Production of Plant Proteases and New Biotechnological Applications: An Updated Review

2022

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An updated review of emerging plant proteases with potential biotechnological application is presented. Plant proteases show comparable or even greater performance than animal or microbial proteases for by‐product valorization through hydrolysis for, for example, cheese whey, bird feathers, collagen, keratinous materials, gelatin, fish protein, and soy protein. Active biopeptides can be obtained as high added value products, which have shown numerous beneficial effects on human health. Plant proteases can also be used for wastewater treatment. The production of new plant proteases is encouraged for the following advantages: low cost of isolation using simple procedures, remarkable stability over a wide range of operating conditions (temperature, pH, salinity, and organic solvents), substantial affinity to a broad variety of substrates, and possibility of immobilization. Vegetable proteases have enormous application potential for the valorization of industrial waste and its conversion into products with high added value through low‐cost processes.

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Plant proteases: from molecular mechanisms to functions in development and immunity

Cited by 22 publications

References 12 publications

Proteolytic and Structural Changes in Rye and Triticale Roots under Aluminum Stress

Proteolytic and Structural Changes in Rye and Triticale Roots under Aluminum Stress

The flax genome reveals orbitide diversity

Production of Plant Proteases and New Biotechnological Applications: An Updated Review

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