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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
Expression of Magnaporthe oryzae genes encoding cysteine-rich proteins secreted during nitrogen starvation and interaction with its host, Oryza sativa.
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Previous studies have shown that the blast fungus, Magnaporthe oryzae, may experience nitrogen starvation during infection of its plant host (rice,Oryza sativa). Here, we studied the expression of seven genes encoding cysteine-rich proteins with N-terminal signal peptides during nitrogen limitation
Molecular characterization of mature pollen-specific genes encoding novel small cysteine-rich proteins in rice (Oryza sativa L.).
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In our previous cDNA microarray analysis, we identified 53 mature anther-specific genes, whose function was unknown, in rice. We reanalyzed these genes from the viewpoint of the specific amino acid motif. Out of 53 genes, three genes, Os-26, Os-32, and Os-169 (renamed as OsSCP1, OsSCP2, and OsSCP3),
l-cysteine desulfhydrase-related H2 S production is involved in OsSE5-promoted ammonium tolerance in roots of Oryza sativa.
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Previous studies revealed that rice heme oxygenase PHOTOPERIOD SENSITIVITY 5 (OsSE5) is involved in the regulation of tolerance to excess ammonium by enhancing antioxidant defence. In this study, the relationship between OsSE5 and hydrogen sulfide (H2 S), a well-known signalling molecule, was
Novel cysteine-rich peptides from Digitaria ciliaris and Oryza sativa enhance tolerance to cadmium by limiting its cellular accumulation.
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By means of functional screening using the cadmium (Cd)-sensitive ycf1 yeast mutant, we have isolated a novel cDNA clone, DcCDT1, from Digitaria ciliaris growing in a former mining area in northern Japan, and have shown that it confers Cd tolerance to the yeast cells, which accumulated almost 2-fold
Domain exchange between Oryza sativa phytochelatin synthases reveals a region that determines responsiveness to arsenic and heavy metals.
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Phytochelatin synthases (PCSs) are activated by toxic metals/metalloids such as cadmium and arsenic and synthesize phytochelatins for detoxification of toxic elements. Rice (Oryza sativa L.) has two PCSs (OsPCS1 and OsPCS2), and we previously revealed that OsPCS1 has a higher responsiveness to
Purification and properties of cysteine protease from rhizomes of Curcuma longa (Linn.).
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BACKGROUND
Turmeric rhizome (Curcuma domestica Linn.) contains proteases and has proteolytic activity. Curcumin from turmeric rhizomes has been used for healing many ailments, including cancer. The purpose of this study was to purify turmeric protease and to research their biochemical
Rapid turnover of antimicrobial-type cysteine-rich protein genes in closely related Oryza genomes.
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Defensive and reproductive protein genes undergo rapid evolution. Small, cysteine-rich secreted peptides (CRPs) act as antimicrobial agents and function in plant intercellular signaling and are over-represented among reproductively expressed proteins. Because of their roles in defense, reproduction
Heterologous expression and metal-binding characterization of a type 1 metallothionein isoform (OsMTI-1b) from rice (Oryza sativa).
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Metallothioneins (MTs) are ubiquitous, low molecular mass and cysteine-rich proteins that play important roles in maintaining intracellular metal homeostasis, eliminating metal toxification and protecting the cells against oxidative damages. MTs are able to bind metal ions through the thiol groups
Copper-induced hydrogen peroxide upregulation of a metallothionein gene, OsMT2c, from Oryza sativa L. confers copper tolerance in Arabidopsis thaliana.
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Metallothioneins (MTs) are low-molecular-weight, cysteine-rich metal-binding proteins found in numerous genera and species, but their functions in abiotic stress tolerance remain unclear. Here, a MT gene from Oryza sativa, OsMT2c, was isolated and characterized, encoding a type 2 MT, and observed
Arsenite tolerance is related to proportional thiolic metabolite synthesis in rice (Oryza sativa L.).
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Thiol metabolism is the primary detoxification strategy by which rice plants tolerate arsenic (As) stress. In light of this, it is important to understand the importance of harmonised thiol metabolism with As accumulation and tolerance in rice plant. For this aim, tolerant (T) and sensitive (S)
Molecular cloning and characterization of RGA1 encoding a G protein alpha subunit from rice (Oryza sativa L. IR-36).
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A cDNA clone, RGA1, was isolated by using a GPA1 cDNA clone of Arabidopsis thaliana G protein alpha subunit as a probe from a rice (Oryza sativa L. IR-36) seedling cDNA library from roots and leaves. Sequence analysis of genomic clone reveals that the RGA1 gene has 14 exons and 13 introns, and
C-terminal extension of calmodulin-like 3 protein from Oryza sativa L.: interaction with a high mobility group target protein.
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A large number of calmodulin-like (CML) proteins are present in plants, but there is little detailed information on the functions of these proteins in rice (Oryza sativa L.). Here, the CML3 protein from rice (OsCML3) and its truncated form lacking the C-terminal extension (OsCML3m) were found to
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
Characterization of allergenic epitopes of Ory s1 protein from Oryza sativa and its homologs.
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Vaccination is the most effective technique suggested now days for allergy treatment. Recombinant-based approaches are mostly focused on genetic modification of allergens to produce molecules with reduced allergenic activity and conserved antigenicity. The molecules developed for vaccination in
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