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Article

Opposing effects of folding and assembly chaperones on evolvability of Rubisco.

Nature chemical biology - 1 Feb 2015

Durão Paulo, Aigner Harald, Nagy Péter, Mueller-Cajar Oliver, Hartl F Ulrich, Hayer-Hartl Manajit

Abstract excerpt

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...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 25558973
DOI: 10.1038/nchembio.1715

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