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Side 1 fra 53 resultater
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
Rice serine/threonine kinase 1 is required for the stimulation of OsNug2 GTPase activity.
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Several GTPases are required for ribosome biogenesis and assembly. We recently identified rice (Oryza sativa) nuclear/nucleolar GTPase 2 (OsNug2), a YlqF/YawG family GTPase, as having a role in pre-60S ribosomal subunit maturation. To investigate the potential factors involved in regulating OsNug2
Export of β-1,3-glucanase from mutant rice cells rechallenged and stressed with lysine plus threonine.
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Mutant rice cells (Oryza sativa L.) grown in liquid suspension cultures exported greater quantities of protein and β-glucanases than controls. These mutants were isolated from anther calli resistant to 1 mM lysine plus threonine (LT), regenerated and reestablished as cell suspension cultures from
Molecular cloning and biochemical characterization of a receptor-like serine/threonine kinase from rice.
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A receptor-like protein kinase, OsPK10, has been cloned from rice (Oryza sativa). The 2.8 kb cDNA contains an open reading frame capable of encoding a peptide sequence of 824 amino acids. The topological features of the predicted OsPK10 protein include an N-terminal signal peptide, a cysteine-rich
Oryza sativa H+-ATPase (OSA) is Involved in the Regulation of Dumbbell-Shaped Guard Cells of Rice.
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The stomatal apparatus consists of a pair of guard cells and regulates gas exchange between the leaf and atmosphere. In guard cells, blue light (BL) activates H(+)-ATPase in the plasma membrane through the phosphorylation of its penultimate threonine, mediating stomatal opening. Although this
Interspecific rice hybrid of Oryza sativa x Oryza nivara reveals a significant increase in seed protein content.
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Wild species offer a potential reservoir of genetic variation for crop improvement. Besides the valuable genes for disease resistance that the wild species have provided for rice improvement, recent studies have shown that these wild species could also provide favorable alleles for the improvement
An epitope of rice threonine- and hydroxyproline-rich glycoprotein is common to cell wall and hydrophobic plasma-membrane glycoproteins.
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A monoclonal antibody, LM1, has been derived that has a high affinity for an epitope of hydroxyproline-rich glycoproteins (HRGPs). In suspension-cultured rice (Oryza sativa L.) cells the epitope is carried by three major proteins with different biochemical properties. The most abundant is the 95-kDa
A Kelch motif-containing serine/threonine protein phosphatase determines the large grain QTL trait in rice.
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A thorough understanding of the genetic basis of rice grain traits is critical for the improvement of rice (Oryza sativa L.) varieties. In this study, we generated an F₂ population by crossing the large-grain japonica cultivar CW23 with Peiai 64 (PA64), an elite indica small-grain cultivar. Using
Novel allelic variant of Lpa1 gene associated with a significant reduction in seed phytic acid content in rice (Oryza sativa L.).
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In plants, myo-inositol-1,2,3,4,5,6-hexakisphosphate (InsP6), also known as phytic acid (PA), is a major component of organic phosphorus (P), and accounts for up to 85% of the total P in seeds. In rice (Oryza sativa L.), PA mainly accumulates in rice bran, and chelates mineral cations, resulting in
Variation in composition, protein and pasting characteristics of different pigmented and non pigmented rice (Oryza sativa L.) grown in Indian Himalayan region.
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This present study was aimed to evaluate proximate composition, antioxidant activity, amino and phenolic acids, protein profile and pasting characteristics of pigmented rice (PR) and non pigmented rice (NPR) landraces grown in Himalayan region. Higher antioxidant activity, total phenolic content,
Phosphorylation of the C2 subunit of the proteasome in rice (Oryza sativa L.).
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Proteasomes function mainly in the ATP-dependent degradation of proteins that have been conjugated with ubiquitin. To demonstrate the phosphorylation of proteasomes in plants, we conducted an enzymatic dephosphorylation experiment with a crude extract of rice cultured cells. The results indicated
Isolation and characterization of a putative transducer of endoplasmic reticulum stress in Oryza sativa.
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Following endoplasmic reticulum (ER) stress that prevents correct folding or assembly of ER proteins, at least three responses occur to maintain cell homeostasis: induction of chaperones, attenuation of protein synthesis, and enhancement of lipid synthesis. Transducers that transmit ER stress to the
barren inflorescence2 Encodes a co-ortholog of the PINOID serine/threonine kinase and is required for organogenesis during inflorescence and vegetative development in maize.
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Organogenesis in plants is controlled by meristems. Axillary meristems, which give rise to branches and flowers, play a critical role in plant architecture and reproduction. Maize (Zea mays) and rice (Oryza sativa) have additional types of axillary meristems in the inflorescence compared to
Production of Marker-free Transgenic Rice (Oryza sativa L.) with Improved Nutritive Quality Expressing AmA1.
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Background: Rice seed proteins are lacking essential amino acids (EAAs). Genetic engineering offers a fast and sustainable method to solve this problem as it allows the specific expression of heterologous EAA-rich proteins. The use of selectable marker gene is essential for generation of transgenic
Structure, evolution and expression of a second subfamily of protein phosphatase 2A catalytic subunit genes in the rice plant (Oryza sativa L.).
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Protein phosphatase 2A (PP2A) is one of the major serine/threonine protein phosphatases in the cell and plays a variety of regulatory roles in metabolism and signal transduction. Previously, we described the structure and expression of two genes encoding PP2A catalytic subunits (PP2Ac)--OsPP2A-1 and
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