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arabidopsis thaliana/protease

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The S8 serine, C1A cysteine and A1 aspartic protease families in Arabidopsis.

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The Arabidopsis thaliana genome has over 550 protease sequences representing all five catalytic types: serine, cysteine, aspartic acid, metallo and threonine (MEROPS peptidase database, http://merops.sanger.ac.uk/), which probably reflect a wide variety of as yet unidentified functions performed by
The grape aspartic protease gene, AP13 was previously reported to be responsive, in Chinese wild Vitis quinquangularis cv. 'Shang-24', to infection by Erysiphe necator, the causal agent of powdery mildew disease, as well as to treatment with salicylic acid in V. labrusca×V. vinifera cv. 'Kyoho'. In

An atypical aspartic protease modulates lateral root development in Arabidopsis thaliana.

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Few atypical aspartic proteases (APs) present in plants have been functionally studied to date despite having been implicated in developmental processes and stress responses. Here we characterize a novel atypical AP that we name Atypical Aspartic Protease in Roots 1 (ASPR1), denoting its expression

Sphingolipid-induced cell death in Arabidopsis is negatively regulated by the papain-like cysteine protease RD21.

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It is now well established that sphingoid Long Chain Bases (LCBs) are crucial mediators of programmed cell death. In plants, the mycotoxin fumonisin B1 (FB1) produced by the necrotrophic fungus Fusarium moniliforme disrupts the sphingolipid biosynthesis pathway by inhibiting the ceramide synthase

Protease inhibitor studies and cloning of a serine carboxypeptidase cDNA from germinating seeds of pea (Pisum sativum L.).

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The nature of the proteolytic activity found within the germinating pea (Pisum sativum) seed, 4 days from the initiation of imbibition, was determined by the use of specific protease inhibitors. These studies have shown most of the activity to belong to metallo or metal-activated and serine
Protease mediated proteolysis has been widely implicated in virulence of necrotrophic fungal pathogens. This is counteracted in plants by evolving new and effective antimicrobial peptides (AMP) that constitute important components of innate immune system. Peptide extraction from rhizome of Zingiber

Mutator-like elements identified in melon, Arabidopsis and rice contain ULP1 protease domains.

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The transposon Mutator was first identified in maize, and is one of the most active mobile elements in plants. The Arabidopsis thaliana genome contains at least 200 Mutator-like elements (MULEs), which contain the Mutator-like transposase gene, and often additional genes. We have detected a novel

The rice OsSAG12-2 gene codes for a functional protease that negatively regulates stress-induced cell death.

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Senescence is the final stage of plant development. Although expression of most of the genes is suppressed during senescence, a set of genes referred as senescence-associated genes (SAGs) is induced. Arabidopsis thaliana SAG12 (AtSAG12) is one such gene that has been mostly studied for its strict

Differential Roles of the Thylakoid Lumenal Deg Protease Homologs in Chloroplast Proteostasis.

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Deg proteases are involved in protein quality control in prokaryotes. Of the three Arabidopsis (Arabidopsis thaliana) homologs, Deg1, Deg5, and Deg8, located in the thylakoid lumen, Deg1 forms a homohexamer, whereas Deg5 and Deg8 form a heterocomplex. Both Deg1 and Deg5-Deg8 were shown separately to

The thylakoid protease Deg1 is involved in photosystem-II assembly in Arabidopsis thaliana.

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DegP proteases have been shown to possess both chaperone and protease activities. The proteolytic activities of chloroplast DegP-like proteases have been well documented. However, whether chloroplast Deg proteases also have chaperone activities has remained unknown. Here we show that chloroplast

The thylakoid lumen protease Deg1 is involved in the repair of photosystem II from photoinhibition in Arabidopsis.

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Deg1 is a Ser protease peripherally attached to the lumenal side of the thylakoid membrane. Its physiological function is unknown, but its localization makes it a suitable candidate for participation in photoinhibition repair by degradation of the photosystem II reaction center protein D1. We
A cDNA, ERD1, isolated from one-hour-dehydrated plants of Arabidopsis thaliana L. encodes a putative protein that is similar to the regulatory ATPase subunit (ClpA) of the Clp protease and contains a putative chloroplast-targeting transit-peptide at the N-terminus. A chimeric gene with the putative

A flowchart to analyze protease activity in plant mitochondria.

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Proteases are one of the most abundant classes of enzymes and are involved in a plethora of biological processes in many cellular compartments, including the mitochondria. To understand the role of proteases is essential to determine their substrate repertoire, preferably in an in vivo setting. In

Re-targeting of a plant defense protease by a cyst nematode effector.

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Plants mount defense responses during pathogen attacks, and robust host defense suppression by pathogen effector proteins is essential for infection success. 4E02 is an effector of the sugar beet cyst nematode Heterodera schachtii. Arabidopsis thaliana lines expressing the effector-coding sequence

Two SUMO proteases SUMO PROTEASE RELATED TO FERTILITY 1 and -2 are required for fertility.

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In plants, the posttranslational modification small ubiquitin-like modifier (SUMO) is involved in regulating several important developmental and cellular processes, including flowering time control and responses to biotic and abiotic stresses. Here, we report two proteases, SUMO PROTEASE RELATED TO
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