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  Opposing effects of folding and assembly chaperones on evolvability of Rubisco

Durao, P., Aigner, H., Nagy, P., Mueller-Cajar, O., Hartl, F. U., & Hayer-Hartl, M. (2015). Opposing effects of folding and assembly chaperones on evolvability of Rubisco. NATURE CHEMICAL BIOLOGY, 11(2), 148-155. doi:10.1038/NCHEMBIO.1715.

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 Urheber:
Durao, Paulo1, Autor           
Aigner, Harald1, Autor           
Nagy, Peter1, Autor           
Mueller-Cajar, Oliver1, Autor           
Hartl, F. Ulrich1, Autor           
Hayer-Hartl, Manajit2, Autor           
Affiliations:
1Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565152              
2Hayer-Hartl, Manajit / Chaperonin-assisted Protein Folding, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565153              

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Schlagwörter: RIBULOSE-BISPHOSPHATE CARBOXYLASE; ESCHERICHIA-COLI; RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE; HEXADECAMERIC RUBISCO; DIRECTED EVOLUTION; PROTEIN EVOLUTION; SEQUENCE SPACE; ENZYME; OXYGENASE; SELECTION
 Zusammenfassung: Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) catalyzes the fixation of CO2 in photosynthesis. Despite its pivotal role, Rubisco is an inefficient enzyme and thus is a key target for directed evolution. Rubisco biogenesis depends on auxiliary factors, including the GroEL/ES-type chaperonin for folding and the chaperone RbcX for assembly. Here we performed directed evolution of cyanobacterial form I Rubisco using a Rubisco-dependent Escherichia coli strain. Overexpression of GroEL/ES enhanced Rubisco solubility and tended to expand the range of permissible mutations. In contrast, the specific assembly chaperone RbcX had a negative effect on evolvability by preventing a subset of mutants from forming holoenzyme. Mutation F140I in the large Rubisco subunit, isolated in the absence of RbcX, increased carboxylation efficiency approximately threefold without reducing CO2 specificity. The F140I mutant resulted in a similar to 55% improved photosynthesis rate in Synechocystis PCC6803. The requirement of specific biogenesis factors downstream of chaperonin may have retarded the natural evolution of Rubisco.

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Sprache(n): eng - English
 Datum: 2015-02
 Publikationsstatus: Erschienen
 Seiten: 10
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: ISI: 000348358800013
DOI: 10.1038/NCHEMBIO.1715
 Art des Abschluß: -

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Titel: NATURE CHEMICAL BIOLOGY
Genre der Quelle: Zeitschrift
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Affiliations:
Ort, Verlag, Ausgabe: 75 VARICK ST, 9TH FLR, NEW YORK, NY 10013-1917 USA : NATURE PUBLISHING GROUP
Seiten: - Band / Heft: 11 (2) Artikelnummer: - Start- / Endseite: 148 - 155 Identifikator: ISSN: 1552-4450