Protein structure and selection pressure in plants: Using mutation to understand the functional importance of protein structure

Authors: Long, Evan; MONROE, GREY - University Of California, Davis

Submitted to: BMC Genomics
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 2/11/2026
Publication Date: 2/24/2026
Citation: Long, E.M., Monroe, G. 2026. Protein structure and selection pressure in plants: Using mutation to understand the functional importance of protein structure. BMC Genomics. https://doi.org/10.1186/s12864-026-12674-2.
DOI: https://doi.org/10.1186/s12864-026-12674-2

Interpretive Summary: Understanding which mutations have impact on plant functions is instrumental to interventions of genetic engineering and breeding. Recent advances in protein structure prediction offers a method to examine where mutations fall on a whole proteome scale. This study examines trends in mutational impact across four plant species: Arabidopsis, rice, cassava, and sugar beet. This analysis offers a method to compare mutational fitness effect with protein structure in plants.

Technical Abstract: Recent advances in protein structure prediction have opened new avenues for understanding the potential impact of genetic mutations and how they might affect protein structure. In this study, we analyzed the distribution and structural characteristics of mutations in four plant species: Arabidopsis, rice, sugar beet, and cassava. We integrated population genotype datasets with protein structure predictions to map mutation positions to their corresponding gene protein products and structural features. Our analysis reveals that high-effect mutations are more likely to occur in unstructured, disordered regions of proteins rather than in well-folded, conserved regions. This finding suggests that natural selection exerts greater pressure to conserve sequence integrity in folded regions, which are crucial for protein function. Conversely, disordered regions may tolerate higher variability exhibiting a higher frequency of impactful mutations. By providing a comprehensive overview of mutation distribution in relation to protein structure, this study enhances our understanding of the evolutionary pressures shaping plant proteomes. The insights gained from this research could inform future studies on protein function, evolutionary biology, and plant improvement strategies.