Rubisco functional integrity requires a dedicated three-step maturation pathway

Proteins generally begin with methionine, which is often removed to expose the second residue. RuBP carboxylase/oxygenase (Rubisco), the most abundant enzyme on Earth and a major carbon and nitrogen reservoir, escapes this paradigm. Its catalytic subunit, RbcL, undergoes unusual amino terminal maturation, including atypical initiator methionine-serine cleavage and proline acetylation, a modification not seen in other biological systems. We define a specialized pathway of two sequential aminopeptidases and an amino terminal acetyltransferase, dedicated to RbcL, that executes processing. This maturation is coupled to chaperone-assisted holoenzyme assembly, enhances activation by Rubisco activase, and shields the complex from degradation during senescence. Disruption of this pathway reduces Rubisco accumulation and catalytic competence, revealing an evolutionarily tailored mechanism integrating protein maturation, assembly, and stability of a central metabolic enzyme.

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Publication Details

Journal
Science Advances
Published
2026-09-09
DOI
https://doi.org/10.1126/sciadv.aeh5060
Primary Topic
Metal-Catalyzed Oxygenation Mechanisms
Type
article
Field-Weighted Citation Impact
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article

Rubisco functional integrity requires a dedicated three-step maturation pathway

Iris Finkemeier, Lucile Jomat, Laïla Sago, Patrick Schall et al.
Science Advances
Metal-Catalyzed Oxygenation Mechanisms
article

Rubisco functional integrity requires a dedicated three-step maturation pathway

Iris Finkemeier, Lucile Jomat, Laïla Sago, Patrick Schall, Jens S Mühlenbeck, Bernhard Grimm, Dong Xie, Frédéric Frottin, J. Boyer, Cyril Dian, Thierry Meinnel, Carmela Giglione, Jürgen Eirich, Yuwei Wang
article en

Abstract

Proteins generally begin with methionine, which is often removed to expose the second residue. RuBP carboxylase/oxygenase (Rubisco), the most abundant enzyme on Earth and a major carbon and nitrogen reservoir, escapes this paradigm. Its catalytic subunit, RbcL, undergoes unusual amino terminal maturation, including atypical initiator methionine-serine cleavage and proline acetylation, a modification not seen in other biological systems. We define a specialized pathway of two sequential aminopeptidases and an amino terminal acetyltransferase, dedicated to RbcL, that executes processing. This maturation is coupled to chaperone-assisted holoenzyme assembly, enhances activation by Rubisco activase, and shields the complex from degradation during senescence. Disruption of this pathway reduces Rubisco accumulation and catalytic competence, revealing an evolutionarily tailored mechanism integrating protein maturation, assembly, and stability of a central metabolic enzyme.

Science AdvancesVol. 12(37)
Centre National de la Recherche Scientifique (FR), Commissariat à l'Énergie Atomique et aux Énergies Alternatives (FR), Université Paris-Saclay (FR), Humboldt-Universität zu Berlin (DE), Institute of Plant Biology and Biotechnology (KZ), Institut de Biologie Intégrative de la Cellule (FR), CEA Paris-Saclay (FR)
Openalex Percentile: Top 24%
Metal-Catalyzed Oxygenation Mechanisms
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