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A Cyanobacterial Screening Platform for Rubisco Mutant Variants.

Ute A Hoffmann1, Anna Z Schuppe2, Axel Knave1

  • 1Department of Protein Science, School of Engineering Sciences in Chemistry, Biotechnology and Health, Science for Life Laboratory, KTH - Royal Institute of Technology, 106 91 Stockholm, Sweden.

ACS Synthetic Biology
|July 7, 2025
PubMed
Summary
This summary is machine-generated.

Researchers engineered a Rubisco enzyme platform in cyanobacteria for improved carbon fixation. This system enhances enzyme stability and resilience, paving the way for accelerated photosynthesis.

Keywords:
Synechocystiscyanobacteriaenzyme engineeringhigh-throughput screeningprotein engineeringrubisco

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Area of Science:

  • Biochemistry
  • Enzyme Engineering
  • Synthetic Biology

Background:

  • Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is crucial for carbon fixation but has limitations like low activity and oxygenation.
  • Enzyme engineering of Rubisco aims to improve its efficiency for enhanced carbon capture and global carbon cycling.
  • Cyanobacteria, like *Synechocystis* sp. PCC 6803, serve as model organisms for studying and engineering Rubisco.

Purpose of the Study:

  • To develop and validate an enzyme engineering and screening platform for Rubisco in *Synechocystis*.
  • To assess the functional replacement of native Form I Rubisco with heterologous Form II Rubisco from *Gallionella*.
  • To engineer improved Rubisco variants with enhanced stability and catalytic efficiency for accelerated carbon fixation.

Main Methods:

  • Established an enzyme engineering platform in *Synechocystis* sp. PCC 6803.
  • Replaced native Form I Rubisco with *Gallionella* Form II Rubisco and assessed growth responses to CO2 and O2.
  • Utilized phylogenetically guided EV mutation and in silico evolution to create a multisite mutagenesis library.
  • Employed competitive growth experiments with deep sequencing to screen Rubisco variants under varying gas conditions.

Main Results:

  • Demonstrated successful replacement of native Rubisco with *Gallionella* Rubisco in *Synechocystis*, altering CO2/O2 sensitivity.
  • Identified a specific amino acid substitution in *Gallionella* Rubisco that enhances thermostability.
  • Observed that this amino acid exchange confers resilience against detrimental mutations.
  • Developed a platform for high-throughput screening of Rubisco variants in a cyanobacterial system.

Conclusions:

  • The developed platform enables efficient screening of Rubisco variants in *Synechocystis*.
  • Engineering efforts successfully improved thermostability and resilience of *Gallionella* Rubisco.
  • This work represents a significant step towards optimizing Rubisco for accelerated carbon fixation in cyanobacteria and potentially chloroplasts.