pepstatin/arabidopsis

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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

Nodulin 41, a novel late nodulin of common bean with peptidase activity.

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BACKGROUND The legume-rhizobium symbiosis requires the formation of root nodules, specialized organs where the nitrogen fixation process takes place. Nodule development is accompanied by the induction of specific plant genes, referred to as nodulin genes. Important roles in processes such as

A probarley lectin processing enzyme purified from Arabidopsis thaliana seeds.

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An aspartic proteinase was purified from the seeds of Arabidopsis thaliana (ecotype RLD) using affinity chromatography on pepstatin-agarose and ion exchange chromatography. The purified enzyme is optimally active at pH 3.5 and completely inhibited by pepstatin A. The purified Arabidopsis aspartic

Expression and characterization of the recombinant aspartic proteinase A1 from Arabidopsis thaliana.

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The present study reports the recombinant expression, purification, and partial characterization of a typical aspartic proteinase from Arabidopsis thaliana (AtAP A1). The cDNA encoding the precursor of AtAP A1 was expressed as a functional protein using the yeast Pichia pastoris. The mature form of

An aspartic proteinase present in seeds cleaves Arabidopsis 2 S albumin precursors in vitro.

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The Arabidopsis thaliana 2 S albumins are examples of vacuolar proteins which undergo intensive posttranslational processing. An in vitro processing assay to screen for processing enzymes present in seeds was developed using an in vitro synthesized 2 S albumin precursor as the substrate. A protease

Structure and function of plant aspartic proteinases.

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Aspartic proteinases of the A1 family are widely distributed among plant species and have been purified from a variety of tissues. They are most active at acidic pH, are specifically inhibited by pepstatin A and contain two aspartic residues indispensible for catalytic activity. The

Characterization of recombinant CDR1, an Arabidopsis aspartic proteinase involved in disease resistance.

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The Arabidopsis thaliana constitutive disease resistance 1 (CDR1) gene product is an aspartic proteinase that has been implicated in disease resistance signaling (Xia, Y., Suzuki, H., Borevitz, J., Blount, J., Guo, Z., Patel, K., Dixon, R. A., and Lamb, C. (2004) EMBO J. 23, 980-988). This

Partial purification and characterization of a Ca(2+)-dependent proteinase from Arabidopsis roots.

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Ca2+, an important intracellular messenger in plants, is implicated in controlling diverse cellular functions by regulating the activity of several enzymes. Here we report the presence of a Ca(2+)-dependent proteinase (CDP) activity in roots of Arabidopsis using in-gel assays (zymograms). The CDP

An extracellular aspartic protease functions in Arabidopsis disease resistance signaling.

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We have used activation tagging with T-DNA carrying cauliflower mosaic virus 35S enhancers to investigate the complex signaling networks underlying disease resistance in Arabidopsis. From a screen of approximately 5000 lines, we identified constitutive disease resistance (CDR1) encoding an

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