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Directing the evolution of Rubisco and Rubisco activase: first impressions of a new tool for photosynthesis research

Mueller-Cajar, Oliver; Whitney, Spencer

Description

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...[Show more]

dc.contributor.authorMueller-Cajar, Oliver
dc.contributor.authorWhitney, Spencer
dc.date.accessioned2015-12-10T22:55:15Z
dc.identifier.issn0166-8595
dc.identifier.urihttp://hdl.handle.net/1885/60025
dc.description.abstractDuring 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.
dc.publisherKluwer Academic Publishers
dc.sourcePhotosynthesis Research
dc.subjectKeywords: rca protein, plant; ribulosebisphosphate carboxylase; vegetable protein; directed molecular evolution; genetic selection; genetics; molecular evolution; photosynthesis; review; Directed Molecular Evolution; Evolution, Molecular; Photosynthesis; Plant Prot Activase; CO2-assimilation; Mutagenesis; Protein evolution; Rubisco; Sequence space
dc.titleDirecting the evolution of Rubisco and Rubisco activase: first impressions of a new tool for photosynthesis research
dc.typeJournal article
local.description.notesImported from ARIES
local.identifier.citationvolume98
dc.date.issued2008
local.identifier.absfor060409 - Molecular Evolution
local.identifier.absfor060107 - Enzymes
local.identifier.ariespublicationu9204316xPUB518
local.type.statusPublished Version
local.contributor.affiliationMueller-Cajar, Oliver, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationWhitney, Spencer, College of Medicine, Biology and Environment, ANU
local.description.embargo2037-12-31
local.bibliographicCitation.startpage667
local.bibliographicCitation.lastpage675
local.identifier.doi10.1007/s11120-008-9324-z
dc.date.updated2016-02-24T11:52:20Z
local.identifier.scopusID2-s2.0-57849104368
local.identifier.thomsonID000261577900057
CollectionsANU Research Publications

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