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Rubisco Assembly: A Research Memoir

  • Harry RoyEmail author
Chapter
Part of the Advances in Photosynthesis and Respiration book series (AIPH, volume 36)

Summary

Rubisco is responsible for net carbon dioxide fixation. Due to the high concentration of oxygen in the atmosphere and the relatively low concentration of carbon dioxide, Rubisco “misfires” frequently, splitting a molecule of ribulose bisphosphate rather than adding carbon to it. Evolution has worked to minimize this tendency, but the strategies have been varied, from slight changes in kinetic properties to wholesale re-organization of leaf anatomy. Rubisco consists of two types of subunits in higher plants, green algae, and certain cyanobacteria. The large (L) subunit is encoded in chloroplast DNA and the small (S) subunit in the nucleus. The discovery that Rubisco is encoded by genes in both the chloroplast and the nucleus of higher plants and green algae has motivated considerable research on the biogenesis and biochemistry of Rubisco. This article describes the role of my laboratory in the study of the assembly mechanism of this important enzyme in higher plants.

Keywords

Large Subunit Small Subunit Subunit mRNA Bundle Sheath Cell Rubisco Large Subunit 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Abbreviations:

CABP

Carboxy – arabinitol – bisphosphate;

(n-)Cpn(x)

Chaperonin (n-) represents a biological source such as a chloroplast, and x is the approximate molecular weight in kDa;

GroEL

Any chaperonin homologous to the E. coli form a tetrade­camer of 60 kDa subunits;

GroES

The co-chaperonin of GroEL that binds to GroEL and facilitates protein folding;

L-subunit or RbcL –

The larger of two subunits of Rubisco of eukaryotes or the catalytic subunit of any Rubisco;

Rubisco

Ribulose 1,5 bisphosphate carboxylase/oxygenase (EC 4.1.1.39);

S-subunit or RbcS

The smaller of two subunits of Rubisco found in eukaryotic organisms

Notes

Acknowledgments

The work in my laboratory has been supported by NIH, NSF, and for the most part the USDA. We got material help and advice from many colleagues, including RJ Ellis, S. Hemmingsen, G Lorimer and TJ Andrews, JC Salerno, and S Gutteridge. On behalf of my co-workers I extend our gratitude to all these and the many others, not specifically mentioned here, who encouraged or reviewed our work. It is fascinating to see the field continuing to expand in so many directions, such as the remarkably detailed elucidation of the mechanism of GroEL which I could not cover in detail here, the molecular genetic analysis of the enzymatic mechanism, and the molecular regulation of the biosynthesis of Rubisco.

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© Springer Science+Business Media Dordrecht 2013

Authors and Affiliations

  1. 1.Biology DepartmentRensselaer Polytechnic InstituteTroyUSA

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