scholarly journals The differential response of photosynthesis to high temperature for a boreal and temperate Populus species relates to differences in Rubisco activation and Rubisco activase properties

2009 ◽  
Vol 30 (1) ◽  
pp. 32-44 ◽  
Author(s):  
M. I. Hozain ◽  
M. E. Salvucci ◽  
M. Fokar ◽  
A. S. Holaday
Keyword(s):  
High Temperature ◽  
Rubisco Activase ◽  
Differential Response ◽  
Populus Species ◽  
Rubisco Activation

scholarly journals Magnesium Application Promotes Rubisco Activation and Contributes to High-Temperature Stress Alleviation in Wheat During the Grain Filling

2021 ◽  
Vol 12 ◽  
Author(s):  
Yuhang Shao ◽  
Shiyu Li ◽  
Lijun Gao ◽  
Chuanjiao Sun ◽  
Jinling Hu ◽  
...  
Keyword(s):  
High Temperature ◽  
Temperature Stress ◽  
Grain Filling ◽  
Rubisco Activase ◽  
High Temperature Stress ◽  
Temperature Cycle ◽  
Wheat Grain ◽  
Rubisco Activity ◽  
The Impact ◽  
Rubisco Activation

Inhibited photosynthesis caused by post-anthesis high-temperature stress (HTS) leads to decreased wheat grain yield. Magnesium (Mg) plays critical roles in photosynthesis; however, its function under HTS during wheat grain filling remains poorly understood. Therefore, in this study, we investigated the effects of Mg on the impact of HTS on photosynthesis during wheat grain filling by conducting pot experiments in controlled-climate chambers. Plants were subjected to a day/night temperature cycle of 32°C/22°C for 5 days during post-anthesis; the control temperature was set at 26°C/16°C. Mg was applied at the booting stage, with untreated plants used as a control. HTS reduced the yield and net photosynthetic rate (Pn) of wheat plants. The maximum carboxylation rate (VCmax), which is limited by Rubisco activity, decreased earlier than the light-saturated potential electron transport rate. This decrease in VCmax was caused by decreased Rubisco activation state under HTS. Mg application reduced yield loss by stabilizing Pn. Rubisco activation was enhanced by increasing Rubisco activase activity following Mg application, thereby stabilizing Pn. We conclude that Mg maintains Rubisco activation, thereby helping to stabilize Pn under HTS.

Analysis of Rubisco Activation Using Tobacco with Antisense Rna to Rubisco Activase

1995 ◽  
pp. 4185-4188
Author(s):  
Edward T. Hammond ◽  
Graham S. Hudson ◽  
T. John Andrews ◽  
Ian E. Woodrow
Keyword(s):  
Antisense Rna ◽  
Rubisco Activase ◽  
Rubisco Activation

Limitation of the Rate of Ribulosebisphosphate Carboxylase Activation by Carbamylation and Ribulosebisphosphate Carboxylase Activase Activity: Development and Tests of a Mechanistic Model

1996 ◽  
Vol 23 (2) ◽  
pp. 141 ◽  
Author(s):  
IE Woodrow ◽  
ME Kelly ◽  
KA Mott
Keyword(s):  
Mechanistic Model ◽  
Large Subunit ◽  
Intercellular Co2 Concentration ◽  
Rubisco Activase ◽  
Photon Flux ◽  
Photon Flux Density ◽  
Bisphosphate Carboxylase ◽  
Ribulosebisphosphate Carboxylase ◽  
Kinetics Of ◽  
Rubisco Activation

A mechanistically-based model of light-mediated activation of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is developed. The model describes the kinetics of Rubisco activation following a relatively rapid increase in photon flux density (PPFD) from an initially low level. Underlying the model is the assumption that there are two slow processes that could potentially limit the rate of light-mediated Rubisco activation. These processes are the addition of the activator CO2 to the large subunit of Rubisco, which is accompanied by a conformational change in the enzyme (carbamylation), and activase-mediated removal of ribulose 1,5-bisphosphate from the inactive form of the enzyme. The contribution of these slow processes to the overall activation kinetics of Rubisco was resolved by measuring Rubisco activation in whole spinach leaves using non-steady-state CO2 exchange. It was found that when the change in PPFD was relatively small and a correspondingly small proportion of the Rubisco pool was activated, the kinetics of activation were highly sensitive to the intercellular CO2 concentration (ci). The apparent rate constant for activation under these conditions was found to be similar to that for the carbamylation of purified spinach Rubisco. When the change in PPFD and the proportion of Rubisco activated was relatively large, however, the kinetics of Rubisco activation were almost completely CO2 insensitive and were consistent with those of an enzyme-catalysed reaction. It is suggested that (1) CO2-insensitive activation reflects the operation of Rubisco activase and (2) the increasing CO2 sensitivity seen as the change in PPFD decreases reflects a transition to limitation by carbamylation.

Regulation of Rubisco activation in antisense plants of tobacco containing reduced levels of Rubisco activase

1998 ◽  
Vol 14 (1) ◽  
pp. 101-110 ◽  
Author(s):  
Edward T. Hammond ◽  
T. John Andrews ◽  
Keith A. Mott ◽  
Ian E. Woodrow
Keyword(s):  
Rubisco Activase ◽  
Rubisco Activation

scholarly journals A role for differential Rubisco activase isoform expression in C 4 bioenergy grasses at high temperature

GCB Bioenergy ◽  
2020 ◽  
Vol 13 (1) ◽  
pp. 211-223
Author(s):  
Sang Yeol Kim ◽  
Rebecca A. Slattery ◽  
Donald R. Ort
Keyword(s):  
High Temperature ◽  
Rubisco Activase ◽  
Bioenergy Grasses ◽  
Isoform Expression

scholarly journals The Plastid Casein Kinase 2 Phosphorylates Rubisco Activase at the Thr-78 Site but Is Not Essential for Regulation of Rubisco Activation State

2016 ◽  
Vol 7 ◽  
Author(s):  
Sang Y. Kim ◽  
Kyle W. Bender ◽  
Berkley J. Walker ◽  
Raymond E. Zielinski ◽  
Martin H. Spalding ◽  
...  
Keyword(s):  
Rubisco Activase ◽  
Casein Kinase ◽  
Casein Kinase 2 ◽  
Rubisco Activation
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