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Pàgina 1 des de 140 resultats
The rubisco small subunit is involved in tobamovirus movement and Tm-2²-mediated extreme resistance.
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The multifunctional movement protein (MP) of Tomato mosaic tobamovirus (ToMV) is involved in viral cell-to-cell movement, symptom development, and resistance gene recognition. However, it remains to be elucidated how ToMV MP plays such diverse roles in plants. Here, we show that ToMV MP interacts
The catalytic properties of hybrid Rubisco comprising tobacco small and sunflower large subunits mirror the kinetically equivalent source Rubiscos and can support tobacco growth.
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Plastomic replacement of the tobacco (Nicotiana tabacum) Rubisco large subunit gene (rbcL) with that from sunflower (Helianthus annuus; rbcL(S)) produced tobacco(Rst) transformants that produced a hybrid Rubisco consisting of sunflower large and tobacco small subunits (L(s)S(t)). The tobacco(Rst)
The role of chloroplast electron transport and metabolites in modulating Rubisco activity in tobacco. Insights from transgenic plants with reduced amounts of cytochrome b/f complex or glyceraldehyde 3-phosphate dehydrogenase.
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Leaf metabolites, adenylates, and Rubisco activation were studied in two transgenic tobacco (Nicotiana tabacum L. cv W38) types. Plants with reduced amounts of cytochrome b/f complex (anti-b/f) have impaired electron transport and a low transthylakoid pH gradient that restrict ATP and NADPH
Functional analysis of the Rubisco large subunit ÂN-methyltransferase promoter from tobacco and its regulation by light in soybean hairy roots.
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The ribulose-1,5-bisphosphate carboxylase/ oxygenase (Rubisco) large subunit (LS) ɛ N-methyltransferase (Rubisco LSMT) catalyzes post-translational methylation of the ɛ-amino group of lysine-14 in the LS of Rubisco. The entire nucleotide sequence for the tobacco (Nicotiana tabacum)
The relationship between CO2-assimilation rate, Rubisco carbamylation and Rubisco activase content in activase-deficient transgenic tobacco suggests a simple model of activase action.
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Transgenic tobacco (Nicotiana tabacum L. cv. W38) plants with an antisense gene directed against the mRNA of ribulose-1,5-bisphosphate carboxylase/ oxygenase (Rubisco) activase were used to examine the relationship between CO2-assimilation rate, Rubisco carbamylation and activase content. Plants
Detection of Rubisco and mycotoxins as potential contaminants of a plantibody against the hepatitis B surface antigen purified from tobacco.
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Antibodies have been one of the proteins widely expressed in tobacco plants for pharmaceutical purposes, which demand contaminant free preparations. Rubisco constitutes 40-60% of tobacco leaf soluble proteins; therefore it is the major potential protein contaminant of plantibodies, while mycotoxins
Regulation of ribulose-1,5-bisphosphate Carboxylase/Oxygenase by carbamylation and 2-carboxyarabinitol 1-phosphate in tobacco: insights from studies of antisense plants containing reduced amounts of rubisco activase
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The regulation of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) activity by 2-carboxyarabinitol 1-phosphate (CA1P) was investigated using gas-exchange analysis of antisense tobacco (Nicotiana tabacum) plants containing reduced levels of Rubisco activase. When an increase in light flux
Acclimation of Rubisco specificity factor to drought in tobacco: discrepancies between in vitro and in vivo estimations.
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In studies about the photosynthesis response to environmental stresses, such as drought, the Rubisco specificity factor (tau) is assumed to be constant or derived indirectly from gas exchange measurements. However, an analysis of the acclimation of tau to drought using in vitro determinations is
Preparation of polyclonal antibodies of Rubisco large and small subunits and their application in the functional analysis of the genes.
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Spinach Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase) large (rbcL) and small (rbcS) subunits were separated by SDS-PAGE, and protein amount and purity were determined by Bradford assay. Polyclonal antibodies against rbcL and rbcS subunit were generated in female BALB/c mice and had no
An acidified thermostabilizing mini-peptide derived from the carboxyl extension of the larger isoform of the plant Rubisco activase.
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Thermostable fusion peptide partners are valuable in engineering thermostability in proteins. We evaluated the Arabidopsis counterpart (AtRAce) and an acidified derivative (mRAce) of the conserved carboxyl extension (RAce) of plant Rubisco activase (RCA) for their thermostabilizing properties in
Evolving Methanococcoides burtonii archaeal Rubisco for improved photosynthesis and plant growth.
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In photosynthesis Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) catalyses the often rate limiting CO2-fixation step in the Calvin cycle. This makes Rubisco both the gatekeeper for carbon entry into the biosphere and a target for functional improvement to enhance photosynthesis and plant
Structure of green-type Rubisco activase from tobacco.
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Rubisco, the enzyme that catalyzes the fixation of atmospheric CO(2) in photosynthesis, is subject to inactivation by inhibitory sugar phosphates. Here we report the 2.95-Å crystal structure of Nicotiana tabacum Rubisco activase (Rca), the enzyme that facilitates the removal of these inhibitors. Rca
Structural studies of Rubisco from tobacco.
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An electron density map of ribulose 1,5-bisphosphate carboxylase-oxygenase (Rubisco) from tobacco (Nicotiana tabacum) has been obtained by X-ray crystallography at a nominal resolution of 0.34 nm. Phases were determined by multiple isomorphous replacement with three heavy atom derivatives and then
Characterization of photosystem II photochemistry in transgenic tobacco plants with lowered Rubisco activase content.
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Rubisco activase plays an important role in the regulation of CO(2) assimilation. However, it is unknown how activase regulates photosystem II (PSII) photochemistry. To investigate the effects of Rubisco activase on PSII photochemistry, we obtained transgenic tobacco (Nicotiana tabacum) plants with
Photosynthesis and growth of tobacco with a substituted bacterial Rubisco mirror the properties of the introduced enzyme.
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Complete replacement, by biolistic plastid transformation, of the hexadecameric ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) of tobacco (Nicotiana tabacum) with the dimeric version from the bacterium, Rhodospirillum rubrum, resulted in fully autotrophic and reproductive tobacco plants
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