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proteinase/padi
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Three-dimensional solution structure of oryzacystatin-I, a cysteine proteinase inhibitor of the rice, Oryza sativa L. japonica.
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The three-dimensional structure of oryzacystatin-I, a cysteine proteinase inhibitor of the rice, Oryza sativa L. japonica, has been determined in solution at pH 6.8 and 25 degrees C by (1)H and (15)N NMR spectroscopy. The main body (Glu13-Asp97) of oryzacystatin-I is well-defined and consists of an
Characterization of a rice (Oryza sativa L.) Bowman-Birk proteinase inhibitor: tightly light regulated induction in response to cut, jasmonic acid, ethylene and protein phosphatase 2A inhibitors.
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The Bowman-Birk (BB) family of proteinase inhibitors (PI), initially reported from legume seeds, and thereafter also from wounded alfalfa and maize leaves appear to be regulated in similar ways as the extensively characterized PI I and PI II family from dicots. Here, we report a first
Heterologous expression and characterization of recombinant OsCDR1, a rice aspartic proteinase involved in disease resistance.
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The Oryza sativa constitutive disease resistance 1 (OsCDR1) gene product is an aspartic proteinase that has been implicated in disease resistance signaling. This apoplastic enzyme is a member of the group of 'atypical' plant aspartic proteinases. Recombinant OsCDR1 expressed in Escherichia coli
A DESD-box helicase functions in salinity stress tolerance by improving photosynthesis and antioxidant machinery in rice (Oryza sativa L. cv. PB1).
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The exact mechanism of helicase-mediated salinity tolerance is not yet understood. We have isolated a DESD-box containing cDNA from Pisum sativum (Pea) and named it as PDH45. It is a unique member of DEAD-box helicase family; containing DESD instead of DEAD/H. PDH45 overexpression driven by
Multiple mode regulation of a cysteine proteinase gene expression in rice.
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In many plants, cysteine proteinases play essential roles in a variety of developmental and physiological processes. In rice (Oryza sativa), REP-1 is a primary cysteine proteinase responsible for the digestion of seed storage proteins to provide nutrients to support the growth of young seedlings. In
Oryzacystatins as the first well-defined cystatins of plant origin and their target proteinases in rice seeds.
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Two cystatins occur in mature seeds of the rice, Oryza sativa L. japonica, which are named oryzacystatin I (OC-I) and oryzacystatin II (OC-II). These are highly homologous to each other and are significantly homologous to cystatin superfamily members of animal origin, especially to family-2
Reduced protease activity in transformed rice cell suspension cultures expressing a proteinase inhibitor.
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In this study, we synthesized a synthetic serine proteinase inhibitor II gene (sPI-II) that harbored the chymotrypsin and trypsin inhibitor domains of the PI-II gene from Nicotiana alata. In an effort to reduce protease activity in a rice cell suspension culture, we first synthesized sPI-II using
Induced expression of oryzain alpha gene encoding a cysteine proteinase under stress conditions.
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Oryzain alpha-A, a cysteine proteinase gene was cloned from rice (Oryza sativa L. cv. Aichi-asahi) leaves infected with Magnaporthe grisea. The protein sequence deduced for oryzain alpha-A shares high identity with that of oryzain alpha, a gene expressed in germinating rice seed. Oryzain alpha-A
Potential value of a rice protein extract, containing proteinaceous inhibitors against cysteine proteinases from Porphyromonas gingivalis, for managing periodontal diseases.
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Arg-specific gingipain (Rgp) is a major pathogenic determinant of Porphyromonas gingivalis which is a major pathogen in periodontal disease. We prepared protein extracts with Rgp-inhibitory activity from polished rice (Oryza sativa) and evaluated the effects of these extracts on the growth and
Oryzacystatin-II, a cystatin from rice (Oryza sativa L. japonica), is a dimeric protein: possible involvement of the interconversion between dimer and monomer in the regulation of the reactivity of oryzacystatin-II.
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We examined the biochemical and structural properties of oryzacystatin-II, a phytocystatin in rice (Oryza sativa L. japonica), under heat-stress conditions. The enzyme inhibitory reactivity of oryzacystatin-II was enhanced by heating in a temperature-dependent manner and reached a maximum level by
Role of jasmonate in the rice (Oryza sativa L.) self-defense mechanism using proteome analysis.
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Exogenously applied jasmonic acid (JA) was used to study changes in protein patterns in rice (Oryza sativa L.) seedling tissues, to classify these changes, and to assign a role for these changes, in order to define the role of JA in the rice self-defense mechanism. High resolution two-dimensional
Oryza sativa drought-, heat-, and salt-induced RING finger protein 1 (OsDHSRP1) negatively regulates abiotic stress-responsive gene expression.
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Plants are sessile and unable to avoid environmental stresses, such as drought, high temperature, and high salinity, which often limit the overall plant growth. Plants have evolved many complex mechanisms to survive these abiotic stresses via post-translational modifications. Recent evidence
Expression analysis of proteinase inhibitor-II under OsRGLP2 promoter in response to wounding and signaling molecules in transgenic Nicotiana benthamiana.
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Proteinase inhibitor-II (PI-II) genes are important defense related genes that play critical regulatory roles in plant growth and development. In the present study, the expression of tomato PI-II gene was investigated under the control of a wound-inducible OsRGLP2 (Oryza sativa root germin like
The amino acid sequence of a 20 kDa bifunctional subtilisin/alpha-amylase inhibitor from bran [correction of brain] of rice (Oryza sativa L.) seeds.
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A 20 kDa bifunctional inhibitor of the microbial proteinase, subtilisin, and the alpha-amylase from the larvae of the red flour beetle (Tribolium castaneum) was purified from bran of rice seeds by saline extraction, precipitation with ammonium sulphate, ion-exchange chromatography on DEAE-Cellulose
Characterization of a stress responsive proteinase inhibitor gene with positive effect in improving drought resistance in rice.
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A full-length cDNA gene, designated Oryza sativa chymotrypsin inhibitor-like 1 (OCPI1), was characterized in rice. The predicted protein of OCPI1 shows very high sequence identity to reported chymotrypsin inhibitors from various plant species. Northern-blot analysis showed that the expression of
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