Directing the evolution of Rubisco and Rubisco activase: first impressions of a new tool for photosynthesis researchReport as inadecuate




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Photosynthesis Research

, Volume 98, Issue 1–3, pp 667–675

First Online: 15 July 2008Received: 30 April 2008Accepted: 26 June 2008

Abstract

During the last decade the practice of laboratory-directed protein evolution has become firmly established as a versatile tool in biochemical research by enabling molecular evolution toward desirable phenotypes or detection of novel structure–function interactions. Applications of this technique in the field of photosynthesis research are still in their infancy, but recently first steps have been reported in the directed evolution of the CO2-fixing enzyme Rubisco and its helper protein Rubisco activase. Here we summarize directed protein evolution strategies and review the progressive advances that have been made to develop and apply suitable selection systems for screening mutant forms of these enzymes that improve the fitness of the host organism. The goal of increasing photosynthetic efficiency of plants by improving the kinetics of Rubisco has been a long-term goal scoring modest successes. We discuss how directed evolution methodologies may one day be able to circumvent the problems encountered during this venture.

KeywordsCO2-assimilation Rubisco Activase Protein evolution Sequence space Mutagenesis Abbreviations2-PG2-Phosphoglycolate

3-PGA3-Phosphoglycerate

L-subunitLarge subunit

ribulose-P2Ribulose-1,5-bisphosphate

RubiscoRibulose-P2 carboxylase-oxygenase

S-subunitSmall subunit

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Author: Oliver Mueller-Cajar - Spencer M. Whitney

Source: https://link.springer.com/







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