2020
DOI: 10.1111/gcbb.12768
|View full text |Cite
|
Sign up to set email alerts
|

A role for differential Rubisco activase isoform expression in C4 bioenergy grasses at high temperature

Abstract: Rubisco requires carbamylation at a lysine residue (K201) within the catalytic site to allow Mg 2+ binding for activation and CO 2 fixation (Cleland et al., 1998). Rubisco incorporates a CO 2 molecule into ribulose-1,5-bisphosphate (RuBP) to generate two molecules of 3-phosphoglyceric acid, which are converted into carbohydrate using photosynthetically produced adenosine triphosphate (ATP) and nicotinamide adenine dinucleotide phosphate. Sugar-phosphate

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

3
21
0

Year Published

2021
2021
2024
2024

Publication Types

Select...
8
1

Relationship

1
8

Authors

Journals

citations
Cited by 24 publications
(24 citation statements)
references
References 75 publications
3
21
0
Order By: Relevance
“…Under WW38, no significant changes on the Rubisco activation state were observed ( Figures 4C,D ), which can be explained by the fact that in maize Rubisco is exclusively located in the chloroplast of BSC, surrounding the vascular tissue, that can offer a superior exposure to the evaporative cooling capacity, buffering the BSC temperature rise ( Lundgren et al, 2014 ; Pignon et al, 2019 ). Another possible explanation is that the long-term acclimation to high temperature experienced by these plants allowed the expression of Rca isoforms more active under high temperature repairing catalytic misfire inhibition, as reported in other studies ( Crafts-Brandner and Salvucci, 2002 ; Yin et al, 2014 ; Zhang et al, 2019 ; Kim et al, 2021 ).…”
Section: Discussionmentioning
confidence: 66%
“…Under WW38, no significant changes on the Rubisco activation state were observed ( Figures 4C,D ), which can be explained by the fact that in maize Rubisco is exclusively located in the chloroplast of BSC, surrounding the vascular tissue, that can offer a superior exposure to the evaporative cooling capacity, buffering the BSC temperature rise ( Lundgren et al, 2014 ; Pignon et al, 2019 ). Another possible explanation is that the long-term acclimation to high temperature experienced by these plants allowed the expression of Rca isoforms more active under high temperature repairing catalytic misfire inhibition, as reported in other studies ( Crafts-Brandner and Salvucci, 2002 ; Yin et al, 2014 ; Zhang et al, 2019 ; Kim et al, 2021 ).…”
Section: Discussionmentioning
confidence: 66%
“…Plants grown in warm environments usually have RCAs that are more thermotolerant 89 91 . In S. viridis , maize, and sorghum, high temperature induces the protein level of RCA_α and the rate of RCA_α induction is associated with the recovery rate of Rubisco activation and photosynthesis 92 . Our results, taken with previously published reports, suggest the heat-induced RCA_α may be the thermotolerant isoform.…”
Section: Discussionmentioning
confidence: 99%
“…Exploiting temperature-induced differential expression of Rca is a potential strategy to accomplish this objective. In many crops, Rca consists of multiple protein isoforms with differing heat sensitivity ( Crafts-Brandner et al , 1997 ; Law et al , 2001 ; Law and Crafts-Brandner, 2001 ; Carmo-Silva et al , 2015 ; Scafaro et al , 2019 ; Kim et al , 2020 ). In bread wheat, altered thermal tolerance between Rca isoforms is conferred by a single amino acid substitution that acts as a thermal and regulatory switch, providing a compelling target for future genome editing efforts ( Scafaro et al , 2019 ; Degen et al , 2020 ).…”
Section: Temperature Response Of Photosynthesis Within the Leaf: The mentioning
confidence: 99%