Shedding light on silica biomineralization by comparative analysis of the silica-associated proteomes from three diatom species

Morphogenesis of the intricate patterns of diatom silica cell walls is a protein-guided process, yet to date only very few such silica biomineralization proteins have been identified. Therefore, it is currently unknown whether all diatoms share conserved proteins of a basal silica forming machinery, and whether unique proteins are responsible for the morphogenesis of species-specific silica patterns. To answer these questions, we extracted proteins from the silica of three diatom species (Thalassiosira pseudonana, Thalassiosira oceanica, and Cyclotella cryptica) by complete demineralization of the cell walls. Liquid chromatography coupled with tandem mass spectrometry (LC-MS/MS) analysis of the extracts identified 92 proteins that we name 'soluble silicome proteins' (SSPs). Surprisingly, no SSPs are common to all three species, and most SSPs showed very low similarity to one another in sequence alignments. In-depth bioinformatics analyses revealed that SSPs could be grouped into distinct classes based on short unconventional sequence motifs whose functions are yet unknown. The results from the in vivo localization of selected SSPs indicates that proteins, which lack sequence homology but share unconventional sequence motifs may exert similar functions in the morphogenesis of the diatom silica cell wall.

Automated summary

This study extracted silica proteins from three diatom species and found that there were no common proteins among them, and most proteins showed low similarity in sequence alignments. Bioinformatic analysis grouped these proteins into different classes based on unconventional sequence motifs, but their functions are still unclear. In vivo localization results of selected proteins suggest that proteins lacking sequence homology but sharing unconventional sequence motifs may have similar functions in diatom silica cell wall morphogenesis.