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Evolution of Rubisco activase gene in plants

Plant Molecular Biology, 2017
Rubisco activase of plants evolved in a stepwise manner without losing its function to adapt to the major evolutionary events including endosymbiosis and land colonization. Rubisco activase is an essential enzyme for photosynthesis, which removes inhibitory sugar phosphates from the active sites of Rubisco, a process necessary for Rubisco activation ...
Ragupathi, Nagarajan, Kulvinder S, Gill
openaire   +2 more sources

Rubisco activase – Rubisco's catalytic chaperone

Photosynthesis Research, 2003
The current status of research on the structure, regulation, mechanism and importance of Rubisco activase is reviewed. The activase is now recognized to be a member of the AAA(+) family, whose members participate in macromolecular complexes that perform diverse chaperone-like functions.
openaire   +2 more sources

The activity of Rubisco’s molecular chaperone, Rubisco activase, in leaf extracts

Photosynthesis Research, 2011
Rubisco frequently undergoes unproductive interactions with its sugar-phosphate substrate that stabilize active sites in an inactive conformation. Restoring catalytic competence to these sites requires the "molecular chiropractic" activity of Rubisco activase (activase).
Carmo-Silva, A. Elizabete   +1 more
openaire   +2 more sources

The regulation of Rubisco by Rubisco activase

Journal of Experimental Botany, 1995
Abstract The activity of Rubisco depends on the conversion of the inactive form (E) to the active form (ECM); the binding of the inhibitors CA1P and RuBP to ECM and E, respectively; and the catalytic formation of inhibitory sugar bisphosphates from the enediol intermediate that precedes carboxylation/oxygenation.
openaire   +1 more source

Removal of redox-sensitive Rubisco Activase does not alter Rubisco regulation in soybean

Photosynthesis Research, 2022
Rubisco activase (Rca) facilitates the catalytic repair of Rubisco, the CO2-fixing enzyme of photosynthesis, following periods of darkness, low to high light transitions or stress. Removal of the redox-regulated isoform of Rubisco activase, Rca-α, enhances photosynthetic induction in Arabidopsis and has been suggested as a strategy for the improvement ...
Christopher M. Harvey   +10 more
openaire   +2 more sources

Structure of green-type Rubisco activase from tobacco

Nature Structural & Molecular Biology, 2011
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.
Stotz, M.   +6 more
openaire   +3 more sources

Heat sensitivity of Rubisco, Rubisco activase and Rubisco binding protein in higher plants

Acta Physiologiae Plantarum, 2004
During the past few years the investigations concerning Rubisco and the changes of its activity and properties at elevated temperature were reconsidered with special reference to the important role of Rubisco activase and Rubisco binding protein. The major changes in Rubisco, Rubisco activase and Rubisco binding protein reported recently are presented ...
Demirevska-Kepova, K, Feller-Kaiser, Urs
openaire   +1 more source

Activation of Ribulose-1,5-bisphosphate Carboxylase/Oxygenase (Rubisco) Involves Rubisco Activase Trp16

Biochemistry, 1996
The role of the N-terminal region of tobacco Rubisco activase in ATP hydrolysis and ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) activation was examined by construction of mutant proteins. Deletion of the first 50 amino acids of Rubisco activase almost completely eliminated the ability to activate Rubisco, without changing the ATP ...
F J, van de Loo, M E, Salvucci
openaire   +2 more sources

The relationship between CO2-assimilation rate, Rubisco carbamylation and Rubisco activase content in activase-deficient transgenic tobacco suggests a simple model of activase action

Planta, 1996
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.
Colleen J, Mate   +4 more
openaire   +2 more sources

Complex formation of rubisco and rubisco activase

Biophysical Journal, 2022
Kazi Waheeda, Po-Lin Chiu
openaire   +1 more source

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