Diversity of Serine Hydrolase Activities of Unchallenged and Botrytis-infected Arabidopsis thaliana

Kaschani, Farnusch; Gu, Christian; Niessen, Sherry; Hoover, Heather; Cravatt, Benjamin F.; Hoorn, Renier A. L. van der

doi:10.1074/mcp.m800494-mcp200

Cited by 93 publications

(106 citation statements)

References 52 publications

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“…SCPL20 is one of the two members of clade IB of the SCPL family, with conserved catalytic triad and carboxylate-binding residues (Fraser et al, 2005). Activity-based protein profiling coupled with Multidimensional Protein Identification Technology (MudPIT) analysis established SCPL20 as a Ser hydrolase (Kaschani et al, 2009). The overexpression allele of SCPL20 is hypersensitive to 10 mM IBA (Supplemental Fig.…”

Section: Revelation Of Peroxisomal Proteolysis In Etiolated Seedlingsmentioning

confidence: 99%

Proteome Analysis of Peroxisomes from Etiolated Arabidopsis Seedlings Identifies a Peroxisomal Protease Involved in β-Oxidation and Development

et al. 2013

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Plant peroxisomes are highly dynamic organelles that mediate a suite of metabolic processes crucial to development. Peroxisomes in seeds/dark-grown seedlings and in photosynthetic tissues constitute two major subtypes of plant peroxisomes, which had been postulated to contain distinct primary biochemical properties. Multiple in-depth proteomic analyses had been performed on leaf peroxisomes, yet the major makeup of peroxisomes in seeds or dark-grown seedlings remained unclear. To compare the metabolic pathways of the two dominant plant peroxisomal subtypes and discover new peroxisomal proteins that function specifically during seed germination, we performed proteomic analysis of peroxisomes from etiolated Arabidopsis (Arabidopsis thaliana) seedlings. The detection of 77 peroxisomal proteins allowed us to perform comparative analysis with the peroxisomal proteome of green leaves, which revealed a large overlap between these two primary peroxisomal variants. Subcellular targeting analysis by fluorescence microscopy validated around 10 new peroxisomal proteins in Arabidopsis. Mutant analysis suggested the role of the cysteine protease RESPONSE TO DROUGHT21A-LIKE1 in b-oxidation, seed germination, and growth. This work provides a much-needed road map of a major type of plant peroxisome and has established a basis for future investigations of peroxisomal proteolytic processes to understand their roles in development and in plant interaction with the environment.

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Section: Revelation Of Peroxisomal Proteolysis In Etiolated Seedlingsmentioning

confidence: 99%

Proteome Analysis of Peroxisomes from Etiolated Arabidopsis Seedlings Identifies a Peroxisomal Protease Involved in β-Oxidation and Development

et al. 2013

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“…All supernatants were combined and concentrated in an Eppendorf SpeedVac to a final volume of approximately 10 mL. Tryptic peptides were analyzed using a Thermo Scientific LTQ XL mass spectrometer and annotated as described previously (Kaschani et al, 2009a).…”

Section: Affinity Purification and Identification Of Labeled Proteinsmentioning

confidence: 99%

Subclassification and Biochemical Analysis of Plant Papain-Like Cysteine Proteases Displays Subfamily-Specific Characteristics

Richau

Kaschani

Verdoes³

et al. 2012

Plant Physiology

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Papain-like cysteine proteases (PLCPs) are a large class of proteolytic enzymes associated with development, immunity, and senescence. Although many properties have been described for individual proteases, the distribution of these characteristics has not been studied collectively. Here, we analyzed 723 plant PLCPs and classify them into nine subfamilies that are present throughout the plant kingdom. Analysis of these subfamilies revealed previously unreported distinct subfamily-specific functional and structural characteristics. For example, the NPIR and KDEL localization signals are distinctive for subfamilies, and the carboxyl-terminal granulin domain occurs in two PLCP subfamilies, in which some individual members probably evolved by deletion of the granulin domains. We also discovered a conserved double cysteine in the catalytic site of SAG12-like proteases and two subfamily-specific disulfides in RD19A-like proteases. Protease activity profiling of representatives of the PLCP subfamilies using novel fluorescent probes revealed striking polymorphic labeling profiles and remarkably distinct pH dependency. Competition assays with peptide-epoxide scanning libraries revealed common and unique inhibitory fingerprints. Finally, we expand the detection of PLCPs by identifying common and organ-specific protease activities and identify previously undetected proteases upon labeling with cell-penetrating probes in vivo. This study provides the plant protease research community with tools for further functional annotation of plant PLCPs.

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“…Using the position of the biotinylated proteins from the strep-HRP blot (van der Hoorn et al, 2004) as guidelines, corresponding regions in the large sample containing gel were excised from lanes 7 and 9 (see Supplemental Figure 12 online). Next, the gel slabs were subjected to the in-gel digestion procedure, and obtained peptide mixes were used for the subsequent nano-liquid chromatography-electrospray ionization-MS/MS analysis (Kaschani et al, 2009a). The mass spectrometer was essentially set up as described by Nickel et al (2012).…”

Section: Large-scale Activity-based Profiling With Dcg-04 and Target mentioning

confidence: 99%

A Maize Cystatin Suppresses Host Immunity by Inhibiting Apoplastic Cysteine Proteases

et al. 2012

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Ustilago maydis is a biotrophic pathogen causing maize (Zea mays) smut disease. Transcriptome profiling of infected maize plants indicated that a gene encoding a putative cystatin (CC9) is induced upon penetration by U. maydis wild type. By contrast, cc9 is not induced after infection with the U. maydis effector mutant Dpep1, which elicits massive plant defenses. Silencing of cc9 resulted in a strongly induced maize defense gene expression and a hypersensitive response to U. maydis wild-type infection. Consequently, fungal colonization was strongly reduced in cc9-silenced plants, while recombinant CC9 prevented salicylic acid (SA)-induced defenses. Protease activity profiling revealed a strong induction of maize Cys proteases in SA-treated leaves, which could be inhibited by addition of CC9. Transgenic maize plants overexpressing cc9-mCherry showed an apoplastic localization of CC9. The transgenic plants showed a block in Cys protease activity and SA-dependent gene expression. Moreover, activated apoplastic Cys proteases induced SA-associated defense gene expression in naïve plants, which could be suppressed by CC9. We show that apoplastic Cys proteases play a pivotal role in maize defense signaling. Moreover, we identified cystatin CC9 as a novel compatibility factor that suppresses Cys protease activity to allow biotrophic interaction of maize with the fungal pathogen U. maydis.

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Diversity of Serine Hydrolase Activities of Unchallenged and Botrytis-infected Arabidopsis thaliana

Cited by 93 publications

References 52 publications

Proteome Analysis of Peroxisomes from Etiolated Arabidopsis Seedlings Identifies a Peroxisomal Protease Involved in β-Oxidation and Development

Proteome Analysis of Peroxisomes from Etiolated Arabidopsis Seedlings Identifies a Peroxisomal Protease Involved in β-Oxidation and Development

Subclassification and Biochemical Analysis of Plant Papain-Like Cysteine Proteases Displays Subfamily-Specific Characteristics

A Maize Cystatin Suppresses Host Immunity by Inhibiting Apoplastic Cysteine Proteases

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