Skip to main navigation menu Skip to main content Skip to site footer
Plant Science Today (PST)

Research Articles

Vol. 12 No. 4 (2025)

Coevolution of RuBisCO in bryophytes: Insights into structural adaptation and terrestrial transition

DOI
https://doi.org/10.14719/pst.8957
Submitted
18 April 2025
Published
20-09-2025 — Updated on 10-10-2025
Versions

Abstract

Research on the molecular evolution of the RuBisCO enzyme's major component in early-diverging terrestrial plants is inadequate. RuBisCO is a highly important enzyme in photosynthesis that catalyses carbon fixation and performs a central role in global carbon cycles. Bryophytes, which include liverworts, hornworts and mosses, provide a unique evolutionary role as some of the earliest earth plants. To find out better insight about the RuBisCO evolution, this study explores the coevolutionary dynamics in bryophytes using previously available sequence data from UniProt. The methodology pipeline includes the alignment of homologous sequences, filtering and data analysis using CoMap v1.5.2 to find out the coevolving residues. Results revealed that 35 coevolving groups were found in the result of CoMap and 35 coevolving residues i.e., amino acids come under category of secondary structural elements and a total 72 amino acids out total 475 amino acid protein was involved in coevolution. The findings revealed significant coevolution in RuBisCO, which primarily involves hydrophobic and uncharged polar residues, enhancing the structural integrity and catalytic efficiency. This coevolution highlights structural integrity and adaptive potential in response to environmental and functional constraints. This study not only advances our understanding of evolutionary history and functional mechanisms of RuBisCO but also opens new avenues for research and applications in plant biology, synthetic biology and environmental science.

References

  1. 1. Andersson I, Backlund A. Structure and function of Rubisco. Plant Physiol Biochem. 2008;46(3):275-91. https://doi.org/10.1016/j.plaphy.2008.01.001
  2. 2. Tcherkez GGB, Farquhar GD, Andrews TJ. Despite slow catalysis and confused substrate specificity, all ribulose bisphosphate carboxylases may be nearly perfectly optimized. Proc Natl Acad Sci U S A. 2006;103(19):7246-51. https://doi.org/10.1073/pnas.0600605103
  3. 3. Spreitzer RJ, Salvucci ME. Rubisco: structure, regulatory interactions, and possibilities for a better enzyme. Annu Rev Plant Biol. 2002;(53):449-75. https://doi.org/10.1146/annurev.arplant.53.100301.135233
  4. 4. Kenrick P, Crane PR. The origin and early diversification of land plants: a cladistic study. 1997;18:936-7.
  5. 5. Graham LE, Cook ME, Busse JS. The origin of plants: body plan changes contributing to a major evolutionary radiation. Proc Natl Acad Sci U S A. 2000;97(9):4535-40. https://doi.org/10.1073/pnas.97.9.4535
  6. 6. Wang ZO, Pollock DD. Coevolutionary patterns in cytochrome c oxidase subunit I depend on structural and functional context. J Mol Evol. 2007;(65):485-95. https://doi.org/10.1007/s00239-007-9018-8
  7. 7. Yeang C-H, Haussler D. Detecting coevolution in and among protein domains. PLoS Comput Biol. 2007;3(11):e211. https://doi.org/10.1371/journal.pcbi.0030211
  8. 8. Dill KA. Dominant forces in protein folding. Biochemistry. 1990;29(31):7133-55. https://doi.org/10.1021/bi00483a001
  9. 9. Anfinsen CB. Principles that govern the folding of protein chains. Science. 1973;181(4096):223-30. https://doi.org/10.1126/science.181.4096.223
  10. 10. Baldwin RL. Energetics of protein folding. J Mol Biol. 2007;371(2):283–301. https://doi.org/10.1016/j.jmb.2007.05.078
  11. 11. Kyte J, Doolittle RF. A simple method for displaying the hydropathic character of a protein. J Mol Biol. 1982;157(1):105-32. https://doi.org/10.1016/00222836(82)90515-0
  12. 12. Parry MAJ, Andralojc PJ, Mitchell RAC, Madgwick PJ, Keys AJ. Manipulation of Rubisco: the amount, activity, function and regulation. J Exp Bot. 2003;54(386):1321-33. https://doi.org/10.1093/jxb/erg141
  13. 13. Sharwood RE, Ghannoum O, Whitney SM. Prospects for improving CO2 fixation in C3-crops through understanding C4-Rubisco biogenesis and catalytic diversity. Curr Opin Plant Biol. 2016;31:135-42. https://doi.org/10.1016/j.pbi.2016.04.002

Downloads

Download data is not yet available.