Transport and Activation of the Vacuolar Aspartic Proteinase Phytepsin in Barley (Hordeum vulgare L.)

Glathe, Stefanie; Kervinen, Jukka; Nimtz, Manfred; Li, Grace H.; Tobin, Gregory J.; Copeland, Terry D.; Ashford, David A.; Wlodawer, Alexander; Costa, Júlia

doi:10.1074/jbc.273.47.31230

Cited by 65 publications

(75 citation statements)

References 27 publications

(26 reference statements)

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“…Posttranslational transport and activation of APs involves complex processing (32), which makes it difficult to determine the subcellular localization of S5 by using a transgenic approach by fusing the protein with a reporter. We used immunogold labeling and transmission electron microscopy (TEM) techniques to assay the subcellular localization of S5, using sections of nucellar tissues where the gene showed relatively high expression.…”

Section: Resultsmentioning

confidence: 99%

A triallelic system of S5 is a major regulator of the reproductive barrier and compatibility of indica–japonica hybrids in rice

Chen

Ding

Ouyang

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

257

238

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Hybrid sterility is a major form of postzygotic reproductive isolation. Although reproductive isolation has been a key issue in evolutionary biology for many decades in a wide range of organisms, only very recently a few genes for reproductive isolation were identified. The Asian cultivated rice (Oryza sativa L.) is divided into two subspecies, indica and japonica. Hybrids between indica and japonica varieties are usually highly sterile. A special group of rice germplasm, referred to as wide-compatibility varieties, is able to produce highly fertile hybrids when crossed to both indica and japonica. In this study, we cloned S5, a major locus for indicajaponica hybrid sterility and wide compatibility, using a map-based cloning approach. We show that S5 encodes an aspartic protease conditioning embryo-sac fertility. The indica (S5-i) and japonica (S5-j) alleles differ by two nucleotides. The wide compatibility gene (S5-n) has a large deletion in the N terminus of the predicted S5 protein, causing subcellular mislocalization of the protein, and thus is presumably nonfunctional. This triallelic system has a profound implication in the evolution and artificial breeding of cultivated rice. Genetic differentiation between indica and japonica would have been enforced because of the reproductive barrier caused by S5-i and S5-j, and species coherence would have been maintained by gene flow enabled by the wide compatibility gene.subspecies of rice ͉ hybrid sterility ͉ wide compatibility ͉ aspartic protease

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Section: Resultsmentioning

confidence: 99%

A triallelic system of S5 is a major regulator of the reproductive barrier and compatibility of indica–japonica hybrids in rice

Chen

Ding

Ouyang

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

257

238

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“…In accordance, using the computational tool STRING (STRING 9.1; http://string-db.org), which detects known and predicted protein interactions, we uncovered APCB1, an aspartyl protease, predicted to interact with BAGP1. Common features of aspartyl proteases include an active site cleft that contains two catalytic aspartic acid residues, acidic pH optima for enzymatic activity, inhibition by pepstatin A, a conserved overall fold, and preferential cleavage specificity for peptide bonds between amino acid residues with bulky hydrophobic side chains (Glathe et al, 1998). APCB1 shares significant sequence similarity to typical aspartyl proteases.…”

Section: Discussionmentioning

confidence: 99%

Aspartyl Protease-Mediated Cleavage of BAG6 Is Necessary for Autophagy and Fungal Resistance in Plants

et al. 2016

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The Bcl-2-associated athanogene (BAG) family is an evolutionarily conserved group of cochaperones that modulate numerous cellular processes. Previously we found that Arabidopsis thaliana BAG6 is required for basal immunity against the fungal phytopathogen Botrytis cinerea. However, the mechanisms by which BAG6 controls immunity are obscure. Here, we address this important question by determining the molecular mechanisms responsible for BAG6-mediated basal resistance. We show that Arabidopsis BAG6 is cleaved in vivo in a caspase-1-like-dependent manner and via a combination of pulldowns, mass spectrometry, yeast two-hybrid assays, and chemical genomics, we demonstrate that BAG6 interacts with a C2 GRAM domain protein (BAGP1) and an aspartyl protease (APCB1), both of which are required for BAG6 processing. Furthermore, fluorescence and transmission electron microscopy established that BAG6 cleavage triggers autophagy in the host that coincides with disease resistance. Targeted inactivation of BAGP1 or APCB1 results in the blocking of BAG6 processing and loss of resistance. Mutation of the cleavage site blocks cleavage and inhibits autophagy in plants; disease resistance is also compromised. Taken together, these results identify a mechanism that couples an aspartyl protease with a molecular cochaperone to trigger autophagy and plant defense, providing a key link between fungal recognition and the induction of cell death and resistance.

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“…The PSI bears no similarities to animal or microbial AP but shows significant sequence similarities with cDNA saposin precursor sequences (4). This saposin-like domain has been shown to be removed entirely or partially during maturation and processing of plant aspartic proteinase precursors (5,6), rendering two-chain mature enzymes with a domain organization similar to that of the mammalian or microbial AP.…”

mentioning

confidence: 98%

Crystal Structure of Cardosin A, a Glycosylated and Arg-Gly-Asp-containing Aspartic Proteinase from the Flowers ofCynara cardunculus L.

Frazão¹,

Bento²,

Costa³

et al. 1999

Journal of Biological Chemistry

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Aspartic proteinases (AP) have been widely studied within the living world, but so far no plant AP have been structurally characterized. The refined cardosin A crystallographic structure includes two molecules, built up by two glycosylated peptide chains (31 and 15 kDa each). The fold of cardosin A is typical within the AP family. The glycosyl content is described by 19 sugar rings attached to Asn-67 and Asn-257. They are localized on the molecular surface away from the conserved active site and show a new glycan of the plant complex type. A hydrogen bond between Gln-126 and Man␤4 renders the monosaccharide oxygen O-2 sterically inaccessible to accept a xylosyl residue, therefore explaining the new type of the identified plant glycan. The Arg-Gly-Asp sequence, which has been shown to be involved in recognition of a putative cardosin A receptor, was found in a loop between two ␤-strands on the molecular surface opposite the active site cleft. Based on the crystal structure, a possible mechanism whereby cardosin A might be orientated at the cell surface of the style to interact with its putative receptor from pollen is proposed. The biological implications of these findings are also discussed. Aspartic proteinases (AP)1 are a class of enzymes (EC 3.4.23) involved in a number of physiological and pathological processes such as blood pressure homeostasis (renin), retroviral infection (human immunodeficiency virus proteinase), hemoglobin degradation in malaria (plasmepsin), intracellular proteolysis (cathepsin D),and digestion (pepsin) (see Ref. 1 for a recent review). Additionally, AP play an important role in the food industry, e.g. the cheese industry (chymosin) or in soya and cocoa processing. Inhibitors of AP enzymes have significant therapeutic potential for treatment of hypertension, AIDS, tumor invasiveness, and peptic ulcer disease. Despite their distribution in the living world, occurring from retrovirus to mammals, aspartic proteinases share significant similarities in primary and tertiary structures. Members of this class display two Asp-Thr/Ser-Gly motifs within their sequences and are specifically inhibited by pepstatin, a peptide produced by Streptomyces. Several high resolution x-ray structures of mammalian, fungal, and retroviral aspartic proteinases are available. The overall three-dimensional structure consists of two domains of similar secondary structure, dominated by orthogonally packed sheets with several small helical segments. In eukaryotic aspartic proteinases each domain contributes one of the two catalytic aspartate residues to form the active site center located at a long and deep cleft between the two domains. Conversely, in retroviral aspartic proteinases, which are dimeric proteins consisting of two identical subunits, each subunit contributes one catalytic aspartate. It is thought therefore that eukaryotic aspartic proteinases have evolved divergently from a primitive dimeric enzyme resembling retroviral proteinases by gene duplication and fusion.Plant AP have been detected, extracted...

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Transport and Activation of the Vacuolar Aspartic Proteinase Phytepsin in Barley (Hordeum vulgare L.)

Cited by 65 publications

References 27 publications

A triallelic system of S5 is a major regulator of the reproductive barrier and compatibility of indica–japonica hybrids in rice

A triallelic system of S5 is a major regulator of the reproductive barrier and compatibility of indica–japonica hybrids in rice

Aspartyl Protease-Mediated Cleavage of BAG6 Is Necessary for Autophagy and Fungal Resistance in Plants

Crystal Structure of Cardosin A, a Glycosylated and Arg-Gly-Asp-containing Aspartic Proteinase from the Flowers ofCynara cardunculus L.

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