Rubisco functional integrity requires a dedicated three-step maturation pathway
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.
Related
- Long-term high temperatures affect seed maturation and seed coat integrity in Brassica napus
- Cell Death of Human Polymorphonuclear Neutrophils Induced by a Pseudomonas aeruginosa Cystic Fibrosis Isolate Requires a Functional Type III Secretion System
- Collapse of embryonic identities and emergence of functional diversity during motor neuron maturation
- De novo Rubisco design with protein language models
- Machine learning–assisted directed evolution of plant Rubisco
BibTeX
@article{xie2026rubisco,
title = {{Rubisco functional integrity requires a dedicated three-step maturation pathway}},
author = {Dong Xie and Jens Mühlenbeck and Patrick Schall and Jean-Baptiste Boyer and Cyril Dian and Laila Sago and Yuwei Wang and Lucile Jomat and Juergen Eirich and Frédéric Frottin and Iris Finkemeier and Bernhard Grimm and Carmela Giglione and Thierry Meinnel},
journal = {Science Advances},
year = {2026},
month = sep,
doi = {10.1126/sciadv.aeh5060},
url = {https://hal.science/hal-05765435v1},
note = {CC BY 4.0},
}
RIS
TY - JOUR
TI - Rubisco functional integrity requires a dedicated three-step maturation pathway
AU - Dong Xie
AU - Jens Mühlenbeck
AU - Patrick Schall
AU - Jean-Baptiste Boyer
AU - Cyril Dian
AU - Laila Sago
AU - Yuwei Wang
AU - Lucile Jomat
AU - Juergen Eirich
AU - Frédéric Frottin
AU - Iris Finkemeier
AU - Bernhard Grimm
AU - Carmela Giglione
AU - Thierry Meinnel
PY - 2026
DA - 2026/09/11
JO - Science Advances
DO - 10.1126/sciadv.aeh5060
UR - https://hal.science/hal-05765435v1
AB - 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.
SN - 2375-2548
ER -