The DOI matches its Crossref record; 25 of the 25 references it cites were found in a registry or an index.
A faster Rubisco with potential to increase photosynthesis in crops
Open accessAbstract
In photosynthetic organisms, d-ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is the major enzyme assimilating atmospheric CO2 into the biosphere. Owing to the wasteful oxygenase activity and slow turnover of Rubisco, the enzyme is among the most important targets for improving the photosynthetic efficiency of vascular plants. It has been anticipated that introducing the CO2-concentrating mechanism (CCM) from cyanobacteria into plants could enhance crop yield. However, the complex nature of Rubisco’s assembly has made manipulation of the enzyme extremely challenging, and attempts to replace it in plants with the enzymes from cyanobacteria and red algae have not been successful. Here we report two transplastomic tobacco lines with functional Rubisco from the cyanobacterium Synechococcus elongatus PCC7942 (Se7942). We knocked out the native tobacco gene encoding the large subunit of Rubisco by inserting the large and small subunit genes of the Se7942 enzyme, in combination with either the corresponding Se7942 assembly chaperone, RbcX, or an internal carboxysomal protein, CcmM35, which incorporates three small subunit-like domains. Se7942 Rubisco and CcmM35 formed macromolecular complexes within the chloroplast stroma, mirroring an early step in the biogenesis of cyanobacterial β-carboxysomes. Both transformed lines were photosynthetically competent, supporting autotrophic growth, and their respective forms of Rubisco had higher rates of CO2 fixation per unit of enzyme than the tobacco control. These transplastomic tobacco lines represent an important step towards improved photosynthesis in plants and will be valuable hosts for future addition of the remaining components of the cyanobacterial CCM, such as inorganic carbon transporters and the β-carboxysome shell proteins.
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Cites
Improving photosynthetic efficiency for greater yield.
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Spectrophotometric characteristics of chlorophylls a and b and their phenophytins in ethanol
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Structure and function of Rubisco
Andersson, I., & Backlund, A. (2008) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2008.01.001 · Cited by 559
Advancing Our Understanding and Capacity to Engineer Nature’s CO2-Sequestering Enzyme, Rubisco
Whitney, S. M., Houtz, R. L., & Alonso, H. (2011) · Plant Physiology · doi:10.1104/pp.110.164814 · Cited by 461
Rubisco activity and regulation as targets for crop improvement
Parry, M. A. J., Andralojc, P. J., Scales, J. C., Salvucci, M. E., Carmo-Silva, A. E., Alonso, H., & Whitney, S. M. (2013) · Journal of Experimental Botany · doi:10.1093/jxb/ers336 · Cited by 432
Self-citationManipulation of Rubisco: the amount, activity, function and regulation
Parry, M. A. J. (2003) · Journal of Experimental Botany · doi:10.1093/jxb/erg141 · Cited by 377
Self-citationThe Development of C 4 Rice: Current Progress and Future Challenges
von Caemmerer, S., Quick, W. P., & Furbank, R. T. (2012) · Science · doi:10.1126/science.1220177 · Cited by 333
Biogenesis of a Bacterial Organelle: The Carboxysome Assembly Pathway
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Rubisco regulation: a role for inhibitors
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Self-citationPrice, G. D., Pengelly, J. J. L., Forster, B., Du, J., Whitney, S. M., von Caemmerer, S., Badger, M. R., Howitt, S. M., & Evans, J. R. (2013) · Journal of Experimental Botany · doi:10.1093/jxb/ers257 · Cited by 229
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Self-citationKerfeld, C. A., Aussignargues, C., Zarzycki, J., Cai, F., & Sutter, M. (2018) · Nature Reviews Microbiology · doi:10.1038/nrmicro.2018.10 · Cited by 445
Sugar Synthesis from CO2 in Escherichia coli
Antonovsky, N., Gleizer, S., Noor, E., Zohar, Y., Herz, E., Barenholz, U., Zelcbuch, L., Amram, S., Wides, A., Tepper, N., et al. (2016) · Cell · doi:10.1016/j.cell.2016.05.064 · Cited by 365
Carbon dots promote the growth and photosynthesis of mung bean sprouts
Wang, H., Zhang, M., Song, Y., Li, H., Huang, H., Shao, M., Liu, Y., & Kang, Z. (2018) · Carbon · doi:10.1016/j.carbon.2018.04.051 · Cited by 328
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Metadata
- Authors
- Lin, M. T., Occhialini, A., Andralojc, P. J., Parry, M. A. J., & Hanson, M. R.
- Venue
- Nature
- Published
- 2014-09
- Volume
- 513
- Issue
- 7519
- Pages
- 547-550
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W1995403970
- Cited by
- 481
- References
- 25
- FWCI
- 18.01
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Lin, M. T., Occhialini, A., Andralojc, P. J., Parry, M. A. J., & Hanson, M. R. (2014). A faster Rubisco with potential to increase photosynthesis in crops. Nature. https://doi.org/10.1038/nature13776
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