ArticleThe Journal of biological chemistry2016
Functional Characterization of Propeptides in Plant Subtilases as Intramolecular Chaperones and Inhibitors of the Mature Protease.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers, 1 of them a synthesis that pooled it.
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Who cites it
18 citing papers in PubMed, 1 synthesis or guideline pooled it.
- The front line of defence: a meta-analysis of apoplastic proteases in plant immunity.Journal of experimental botany · 2021Pooled it
- The lowdown on breakdown: Open questions in plant proteolysis.The Plant cell · 2024Review
- Phytaspase Does Not Require Proteolytic Activity for Its Stress-Induced Internalization.International journal of molecular sciences · 2024Article
- Prodomain-driven enzyme dimerization: a pH-dependent autoinhibition mechanism that controlsmBio · 2024Article
- Phytaspase Is Capable of Detaching the Endoplasmic Reticulum Retrieval Signal from Tobacco Calreticulin-3.International journal of molecular sciences · 2023Article
- High selectivity of the hyperthermophilic subtilase propeptide domain toward inhibition of its cognate protease.Microbiology spectrum · 2023Article
- Assay for Phytaspase-mediated Peptide Precursor Cleavage Using Synthetic Oligopeptide Substrates.Bio-protocol · 2023Article
- Microbial proteases and their applications.Frontiers in microbiology · 2023Review
- A secreted fungal subtilase interferes with rice immunity via degradation of SUPPRESSOR OF G2 ALLELE OF skp1.Plant physiology · 2022Article
- Identification of Cognate Protease/Substrate Pairs by Use of Class-Specific Inhibitors.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Article
- Sulfated plant peptide hormones.Journal of experimental botany · 2019Review
- Do proteolytic cascades exist in plants?Journal of experimental botany · 2019Review
- The tomato subtilase family includes several cell death-related proteinases with caspase specificity.Scientific reports · 2018Article
- Tobacco phytaspase: Successful expression in a heterologous system.Bioengineered · 2017Article
- Rotational restriction of nascent peptides as an essential element of co-translational protein folding: possible molecular players and structural consequences.Biology direct · 2017Article
- A novel subtilase inhibitor in plants shows structural and functional similarities to protease propeptides.The Journal of biological chemistry · 2017Article
- A non canonical subtilase attenuates the transcriptional activation of defence responses ineLife · 2016Article
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4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Subtilisin-like serine proteases (SBTs) are extracellular proteases that depend on their propeptides for zymogen maturation and activation. The function of propeptides in plant SBTs is poorly understood and was analyzed here for the propeptide of tomato subtilase 3 (SBT3PP). SBT3PP was found to be required as an intramolecular chaperone for zymogen maturation and secretion of SBT3 in vivo Secretion was impaired in a propeptide-deletion mutant but could be restored by co-expression of the propeptide in trans SBT3 was inhibited by SBT3PP with a Kd of 74 nm for the enzyme-inhibitor complex. With a melting point of 87 °C, thermal stability of the complex was substantially increased as compared with the free protease suggesting that propeptide binding stabilizes the structure of SBT3. Even closely related propeptides from other plant SBTs could not substitute for SBT3PP as a folding assistant or autoinhibitor, revealing high specificity for the SBT3-SBT3PP interaction. Separation of the chaperone and inhibitor functions of SBT3PP in a domain-swap experiment indicated that they are mediated by different regions of the propeptide and, hence, different modes of interaction with SBT3. Release of active SBT3 from the autoinhibited complex relied on a pH-dependent cleavage of the propeptide at Asn-38 and Asp-54. The remarkable stability of the autoinhibited complex and pH dependence of the secondary cleavage provide means for stringent control of SBT3 activity, to ensure that the active enzyme is not released before it reaches the acidic environment of the trans-Golgi network or its final destination in the cell wall.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.