Structural plasticity enables evolution and innovation of RuBisCO assemblies-Reference-Cited by-同舟云学术

Structural plasticity enables evolution and innovation of RuBisCO assemblies

Published:2022-08-26 Issue:34 Volume:8 Page:
ISSN:2375-2548
Container-title:Science Advances
language:en
Short-container-title:Sci. Adv.

Author:

Liu Albert K.¹²³^ORCID,Pereira Jose H.⁴⁵^ORCID,Kehl Alexander J.⁶^ORCID,Rosenberg Daniel J.⁵⁷^ORCID,Orr Douglas J.⁸^ORCID,Chu Simon K. S.⁶,Banda Douglas M.²^ORCID,Hammel Michal⁵^ORCID,Adams Paul D.⁴⁵⁹^ORCID,Siegel Justin B.¹⁰¹¹¹²^ORCID,Shih Patrick M.¹²¹³¹⁴^ORCID

Affiliation:

1. Department of Plant and Microbial Biology, University of California, Berkeley, Berkeley, CA 94720, USA.

2. Environmental Genomics and Systems Biology Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.

3. Biochemistry, Molecular, Cellular and Developmental Biology Graduate Group, University of California, Davis, Davis, CA 95616, USA.

4. Technology Division, Joint BioEnergy Institute, Emeryville, CA 94608, USA.

5. Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, 94720, USA.

6. Biophysics Graduate Group, University of California, Davis, Davis, CA, USA.

7. Graduate Group in Biophysics, University of California, Berkeley, Berkeley, CA 94720, USA.

8. Lancaster Environment Centre, Lancaster University, Lancaster LA1 4YQ, UK.

9. Department of Bioengineering, University of California, Berkeley, Berkeley, CA 94720, USA.

10. Genome Center, University of California, Davis, Davis, CA 95616, USA.

11. Chemistry Department, University of California, Davis, Davis, CA 95616, USA.

12. Department of Biochemistry and Molecular Medicine, University of California, Sacramento, Sacramento, CA 95616, USA.

13. Feedstocks Division, Joint BioEnergy Institute, Emeryville, CA 94608, USA.

14. Innovative Genomics Institute, University of California, Berkeley, Berkeley, CA 94720, USA.

Abstract

Oligomerization is a core structural feature that defines the form and function of many proteins. Most proteins form molecular complexes; however, there remains a dearth of diversity-driven structural studies investigating the evolutionary trajectory of these assemblies. Ribulose-1,5-bisphosphate carboxylase-oxygenase (RuBisCO) is one such enzyme that adopts multiple assemblies, although the origins and distribution of its different oligomeric states remain cryptic. Here, we retrace the evolution of ancestral and extant form II RuBisCOs, revealing a complex and diverse history of oligomerization. We structurally characterize a newly discovered tetrameric RuBisCO, elucidating how solvent-exposed surfaces can readily adopt new interactions to interconvert or give rise to new oligomeric states. We further use these principles to engineer and demonstrate how changes in oligomerization can be mediated by relatively few mutations. Our findings yield insight into how structural plasticity may give rise to new oligomeric states.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference70 articles.

1. Structure elucidation of the elusive Enzyme I monomer reveals the molecular mechanisms linking oligomerization and enzymatic activity

2. Directed evolution combined with rational design increases activity of GpdQ toward a non-physiological substrate and alters the oligomeric structure of the enzyme

3. A hydrophobic ratchet entrenches molecular complexes

4. Irremediable Complexity?

5. Evolutionary diversification of the multimeric states of proteins

Cited by 9 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Engineering Rubisco to enhance CO2 utilization;Synthetic and Systems Biotechnology;2024-03

2. Layered entrenchment maintains essentiality in protein-protein interactions;2024-01-20

3. Deep-branching evolutionary intermediates reveal structural origins of form I rubisco;Current Biology;2023-12

4. A Bacterial Form I’ Rubisco Has a Smaller Carbon Isotope Fractionation than Its Form I Counterpart;Biomolecules;2023-03-26

5. Bacterial Form I’ rubisco has smaller carbon isotope fractionation than its Form I counterpart;2023-03-02