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Biochemical characterization of predicted Precambrian RuBisCO

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Biochemical characterization of predicted Precambrian RuBisCO. / Shih, Patrick M.; Occhialini, Alessandro; Cameron, Jeffrey C. et al.
In: Nature Communications, Vol. 7, 10382, 21.01.2016.

Research output: Contribution to Journal/MagazineJournal articlepeer-review

Harvard

Shih, PM, Occhialini, A, Cameron, JC, Andralojc, PJ, Parry, MAJ & Kerfeld, CA 2016, 'Biochemical characterization of predicted Precambrian RuBisCO', Nature Communications, vol. 7, 10382. https://doi.org/10.1038/ncomms10382

APA

Shih, P. M., Occhialini, A., Cameron, J. C., Andralojc, P. J., Parry, M. A. J., & Kerfeld, C. A. (2016). Biochemical characterization of predicted Precambrian RuBisCO. Nature Communications, 7, Article 10382. https://doi.org/10.1038/ncomms10382

Vancouver

Shih PM, Occhialini A, Cameron JC, Andralojc PJ, Parry MAJ, Kerfeld CA. Biochemical characterization of predicted Precambrian RuBisCO. Nature Communications. 2016 Jan 21;7:10382. doi: 10.1038/ncomms10382

Author

Shih, Patrick M. ; Occhialini, Alessandro ; Cameron, Jeffrey C. et al. / Biochemical characterization of predicted Precambrian RuBisCO. In: Nature Communications. 2016 ; Vol. 7.

Bibtex

@article{04c21915a65a42f0971d610a5e5dd98e,
title = "Biochemical characterization of predicted Precambrian RuBisCO",
abstract = "The antiquity and global abundance of the enzyme, RuBisCO, attests to the crucial and longstanding role it has played in the biogeochemical cycles of Earth over billions of years. The counterproductive oxygenase activity of RuBisCO has persisted over billions of years of evolution, despite its competition with the carboxylase activity necessary for carbon fixation, yet hypotheses regarding the selective pressures governing RuBisCO evolution have been limited to speculation. Here we report the resurrection and biochemical characterization of ancestral RuBisCOs, dating back to over one billion years ago (Gyr ago). Our findings provide an ancient point of reference revealing divergent evolutionary paths taken by eukaryotic homologues towards improved specificity for CO2, versus the evolutionary emphasis on increased rates of carboxylation observed in bacterial homologues. Consistent with these distinctions, in vivo analysis reveals the propensity of ancestral RuBisCO to be encapsulated into modern-day carboxysomes, bacterial organelles central to the cyanobacterial CO2 concentrating mechanism.",
author = "Shih, {Patrick M.} and Alessandro Occhialini and Cameron, {Jeffrey C.} and Andralojc, {P. John} and Parry, {Martin A. J.} and Kerfeld, {Cheryl A.}",
year = "2016",
month = jan,
day = "21",
doi = "10.1038/ncomms10382",
language = "English",
volume = "7",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "Nature Publishing Group",

}

RIS

TY - JOUR

T1 - Biochemical characterization of predicted Precambrian RuBisCO

AU - Shih, Patrick M.

AU - Occhialini, Alessandro

AU - Cameron, Jeffrey C.

AU - Andralojc, P. John

AU - Parry, Martin A. J.

AU - Kerfeld, Cheryl A.

PY - 2016/1/21

Y1 - 2016/1/21

N2 - The antiquity and global abundance of the enzyme, RuBisCO, attests to the crucial and longstanding role it has played in the biogeochemical cycles of Earth over billions of years. The counterproductive oxygenase activity of RuBisCO has persisted over billions of years of evolution, despite its competition with the carboxylase activity necessary for carbon fixation, yet hypotheses regarding the selective pressures governing RuBisCO evolution have been limited to speculation. Here we report the resurrection and biochemical characterization of ancestral RuBisCOs, dating back to over one billion years ago (Gyr ago). Our findings provide an ancient point of reference revealing divergent evolutionary paths taken by eukaryotic homologues towards improved specificity for CO2, versus the evolutionary emphasis on increased rates of carboxylation observed in bacterial homologues. Consistent with these distinctions, in vivo analysis reveals the propensity of ancestral RuBisCO to be encapsulated into modern-day carboxysomes, bacterial organelles central to the cyanobacterial CO2 concentrating mechanism.

AB - The antiquity and global abundance of the enzyme, RuBisCO, attests to the crucial and longstanding role it has played in the biogeochemical cycles of Earth over billions of years. The counterproductive oxygenase activity of RuBisCO has persisted over billions of years of evolution, despite its competition with the carboxylase activity necessary for carbon fixation, yet hypotheses regarding the selective pressures governing RuBisCO evolution have been limited to speculation. Here we report the resurrection and biochemical characterization of ancestral RuBisCOs, dating back to over one billion years ago (Gyr ago). Our findings provide an ancient point of reference revealing divergent evolutionary paths taken by eukaryotic homologues towards improved specificity for CO2, versus the evolutionary emphasis on increased rates of carboxylation observed in bacterial homologues. Consistent with these distinctions, in vivo analysis reveals the propensity of ancestral RuBisCO to be encapsulated into modern-day carboxysomes, bacterial organelles central to the cyanobacterial CO2 concentrating mechanism.

U2 - 10.1038/ncomms10382

DO - 10.1038/ncomms10382

M3 - Journal article

C2 - 26790750

VL - 7

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

M1 - 10382

ER -