Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/84538
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dc.contributor.authorLoganathan, Nitinen
dc.contributor.authorTsai, Yi-Chin Candaceen
dc.contributor.authorMueller-Cajar, Oliveren
dc.date.accessioned2017-08-16T07:42:18Zen
dc.date.accessioned2019-12-06T15:46:48Z-
dc.date.available2017-08-16T07:42:18Zen
dc.date.available2019-12-06T15:46:48Z-
dc.date.issued2016en
dc.identifier.citationLoganathan, N., Tsai, Y.-C. C., & Mueller-Cajar, O. (2016). Characterization of the heterooligomeric red-type rubisco activase from red algae. Proceedings of the National Academy of Sciences of the United States of America, 113(49), 14019-14024.en
dc.identifier.issn2784-2400en
dc.identifier.urihttps://hdl.handle.net/10356/84538-
dc.description.abstractThe photosynthetic CO2-fixing enzyme ribulose 1,5-bisphosphate carboxylase/oxygenase (rubisco) is inhibited by nonproductive binding of its substrate ribulose-1,5-bisphosphate (RuBP) and other sugar phosphates. Reactivation requires ATP-hydrolysis–powered remodeling of the inhibited complexes by diverse molecular chaperones known as rubisco activases (Rcas). Eukaryotic phytoplankton of the red plastid lineage contain so-called red-type rubiscos, some of which have been shown to possess superior kinetic properties to green-type rubiscos found in higher plants. These organisms are known to encode multiple homologs of CbbX, the α-proteobacterial red-type activase. Here we show that the gene products of two cbbX genes encoded by the nuclear and plastid genomes of the red algae Cyanidioschyzon merolae are nonfunctional in isolation, but together form a thermostable heterooligomeric Rca that can use both α-proteobacterial and red algal-inhibited rubisco complexes as a substrate. The mechanism of rubisco activation appears conserved between the bacterial and the algal systems and involves threading of the rubisco large subunit C terminus. Whereas binding of the allosteric regulator RuBP induces oligomeric transitions to the bacterial activase, it merely enhances the kinetics of ATP hydrolysis in the algal enzyme. Mutational analysis of nuclear and plastid isoforms demonstrates strong coordination between the subunits and implicates the nuclear-encoded subunit as being functionally dominant. The plastid-encoded subunit may be catalytically inert. Efforts to enhance crop photosynthesis by transplanting red algal rubiscos with enhanced kinetics will need to take into account the requirement for a compatible Rca.en
dc.description.sponsorshipMOE (Min. of Education, S’pore)en
dc.format.extent24 p.en
dc.language.isoenen
dc.relation.ispartofseriesProceedings of the National Academy of Sciences of the United States of Americaen
dc.rights© 2016 The Author(s). This is the author created version of a work that has been peer reviewed and accepted for publication in Proceedings of the National Academy of Sciences of the United States of America, published by National Academy of Sciences on behalf of The Author(s). It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document.  The published version is available at: [http://dx.doi.org/10.1073/pnas.1610758113].en
dc.subjectRubiscoen
dc.subjectActivaseen
dc.titleCharacterization of the heterooligomeric red-type rubisco activase from red algaeen
dc.typeJournal Articleen
dc.contributor.schoolSchool of Biological Sciencesen
dc.identifier.doi10.1073/pnas.1610758113en
dc.description.versionAccepted versionen
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