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Differential pairings of MAT1-1-1 and MAT1-2-1 protein variants with heteromorphic tertiary structures produced by Ophiocordyceps sinensis strains

Li, X.-Z.; Li, Y.-L.; Liu, W.; ZHU, J.-S.

2026-02-16 biochemistry
10.64898/2026.02.16.706022 bioRxiv
Show abstract

The MAT_HMGbox domain in the MAT1-1-1 protein and the HMG-box_ROX1-like domain in the MAT1-2-1 protein play essential roles in DNA binding and regulating the transcription of genes that control sexual reproduction in Ophiocordyceps sinensis. Previous studies have documented differential occurrences, differential transcription, and alternative splicing of the MAT1-1-1 and MAT1-2-1 and pheromone receptor genes in Hirsutella sinensis (Genotype #1 among 17 genome-independent O. sinensis genotypic fungi). This study further revealed that the DNA-binding domains of the paired MAT1-1-1 and MAT1-2-1 proteins derived from each of the 20 O. sinensis strains exhibit heteromorphic tertiary structures, as predicted by AlphaFold 3D structural modeling. The differentially paired mating proteins, characterized by different truncations, 1-4 amino acid substitutions at distinct sites, altered hydrophobicity and secondary structures, and heteromorphic tertiary structures, indicate divergency in the fungal origins of the mating proteins within the mycologically and genetically impure O. sinensis strains. These findings support the hypothesis of O. sinensis self-sterility and are likely ensure the fidelity and genetic diversity of heterothallic or hybrid reproduction throughout the lifecycle of the Cordyceps sinensis insect-fungal complex.

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