Literature DB >> 23162118

Rubisco activity and regulation as targets for crop improvement.

Martin A J Parry1, P John Andralojc, Joanna C Scales, Michael E Salvucci, A Elizabete Carmo-Silva, Hernan Alonso, Spencer M Whitney.   

Abstract

Rubisco (ribulose-1,5-bisphosphate (RuBP) carboxylase/oxygenase) enables net carbon fixation through the carboxylation of RuBP. However, some characteristics of Rubisco make it surprisingly inefficient and compromise photosynthetic productivity. For example, Rubisco catalyses a wasteful reaction with oxygen that leads to the release of previously fixed CO(2) and NH(3) and the consumption of energy during photorespiration. Furthermore, Rubisco is slow and large amounts are needed to support adequate photosynthetic rates. Consequently, Rubisco has been studied intensively as a prime target for manipulations to 'supercharge' photosynthesis and improve both productivity and resource use efficiency. The catalytic properties of Rubiscos from diverse sources vary considerably, suggesting that changes in turnover rate, affinity, or specificity for CO(2) can be introduced to improve Rubisco performance in specific crops and environments. While attempts to manipulate plant Rubisco by nuclear transformation have had limited success, modifying its catalysis by targeted changes to its catalytic large subunit via chloroplast transformation have been much more successful. However, this technique is still in need of development for most major food crops including maize, wheat, and rice. Other bioengineering approaches for improving Rubisco performance include improving the activity of its ancillary protein, Rubisco activase, in addition to modulating the synthesis and degradation of Rubisco's inhibitory sugar phosphate ligands. As the rate-limiting step in carbon assimilation, even modest improvements in the overall performance of Rubisco pose a viable pathway for obtaining significant gains in plant yield, particularly under stressful environmental conditions.

Entities:  

Mesh:

Substances:

Year:  2012        PMID: 23162118     DOI: 10.1093/jxb/ers336

Source DB:  PubMed          Journal:  J Exp Bot        ISSN: 0022-0957            Impact factor:   6.992


  106 in total

1.  Isotopically nonstationary 13C flux analysis of changes in Arabidopsis thaliana leaf metabolism due to high light acclimation.

Authors:  Fangfang Ma; Lara J Jazmin; Jamey D Young; Doug K Allen
Journal:  Proc Natl Acad Sci U S A       Date:  2014-11-03       Impact factor: 11.205

Review 2.  Photorespiration and nitrate assimilation: a major intersection between plant carbon and nitrogen.

Authors:  Arnold J Bloom
Journal:  Photosynth Res       Date:  2014-11-04       Impact factor: 3.573

3.  Structure and mechanism of the Rubisco-assembly chaperone Raf1.

Authors:  Thomas Hauser; Javaid Y Bhat; Goran Miličić; Petra Wendler; F Ulrich Hartl; Andreas Bracher; Manajit Hayer-Hartl
Journal:  Nat Struct Mol Biol       Date:  2015-08-03       Impact factor: 15.369

4.  Detecting long-term metabolic shifts using isotopomers: CO2-driven suppression of photorespiration in C3 plants over the 20th century.

Authors:  Ina Ehlers; Angela Augusti; Tatiana R Betson; Mats B Nilsson; John D Marshall; Jürgen Schleucher
Journal:  Proc Natl Acad Sci U S A       Date:  2015-12-07       Impact factor: 11.205

5.  Variation in Rubisco content and activity under variable climatic factors.

Authors:  Jeroni Galmés; Iker Aranjuelo; Hipólito Medrano; Jaume Flexas
Journal:  Photosynth Res       Date:  2013-06-08       Impact factor: 3.573

6.  Photosynthetic characterization of Rubisco transplantomic lines reveals alterations on photochemistry and mesophyll conductance.

Authors:  Jeroni Galmés; Juan Alejandro Perdomo; Jaume Flexas; Spencer M Whitney
Journal:  Photosynth Res       Date:  2013-05-24       Impact factor: 3.573

7.  Role of small subunit in mediating assembly of red-type form I Rubisco.

Authors:  Jidnyasa Joshi; Oliver Mueller-Cajar; Yi-Chin C Tsai; F Ulrich Hartl; Manajit Hayer-Hartl
Journal:  J Biol Chem       Date:  2014-11-04       Impact factor: 5.157

8.  Opposing effects of folding and assembly chaperones on evolvability of Rubisco.

Authors:  Paulo Durão; Harald Aigner; Péter Nagy; Oliver Mueller-Cajar; F Ulrich Hartl; Manajit Hayer-Hartl
Journal:  Nat Chem Biol       Date:  2015-01-05       Impact factor: 15.040

9.  Assembly-disassembly is coupled to the ATPase cycle of tobacco Rubisco activase.

Authors:  Andrew J Serban; Isabella L Breen; Hoang Q Bui; Marcia Levitus; Rebekka M Wachter
Journal:  J Biol Chem       Date:  2018-10-23       Impact factor: 5.157

10.  Regulation of ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) activase: product inhibition, cooperativity, and magnesium activation.

Authors:  Suratna Hazra; J Nathan Henderson; Kevin Liles; Matthew T Hilton; Rebekka M Wachter
Journal:  J Biol Chem       Date:  2015-08-17       Impact factor: 5.157

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.