Rubisco is evolving for improved catalytic efficiency and CO2 assimilation in plants

• 成果类型: Article
• 署名作者: Bouvier, Jacques W.; Emms, David M.; Kelly, Steven
• 署名单位: University of Oxford
• 刊物名称: PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
• ISSN/ISSBN: 0027-15411
• DOI: 10.1073/pnas.2321050121
• 发表日期: 2024-03-12
• 关键词: ribulose-1; 5-bisphosphate carboxylase-oxygenase; ribulose 1; 5-bisphosphate carboxylase/oxygenase; small-subunit; form-i; antisense rbcs; co2-concentrating mechanisms; evolutionary relationships; substrate-specificity; directed mutagenesis; photosynthetic rate

摘要

Rubisco is the primary entry point for carbon into the biosphere. However, rubisco is widely regarded as inefficient leading many to question whether the enzyme can adapt to become a better catalyst. Through a phylogenetic investigation of the molecular and kinetic evolution of Form I rubisco we uncover the evolutionary trajectory of rubisco kinetic evolution in angiosperms. We show that rbcL is among the 1% of slowest- evolving genes and enzymes on Earth, accumulating one nucleotide substitution every 0.9 My and one amino acid mutation every 7.2 My. Despite this, rubisco catalysis has been continually evolving toward improved CO2/O2 specificity, carboxylase turnover, and carboxylation efficiency. Consistent with this kinetic adaptation, increased rubisco evolution has led to a concomitant improvement in leaf - level CO2 assimilation. Thus, rubisco has been slowly but continually evolving toward improved catalytic efficiency and CO2 assimilation in plants.