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Appears in Collections:Biological and Environmental Sciences Journal Articles
Peer Review Status: Refereed
Title: Shedding light on silica biomineralization by comparative analysis of the silica‐associated proteomes from three diatom species
Author(s): Skeffington, Alastair W
Gentzel, Marc
Ohara, Andre
Milentyev, Alexander
Heintze, Christoph
Böttcher, Lorenz
Görlich, Stefan
Shevchenko, Andrej
Poulsen, Nicole
Kröger, Nils
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Keywords: biosilica
silica morphogenesis
intrinsically disordered proteins
GFP tagging
Thalassiosira pseudonana
Issue Date: Jun-2022
Date Deposited: 28-Jun-2023
Citation: Skeffington AW, Gentzel M, Ohara A, Milentyev A, Heintze C, Böttcher L, Görlich S, Shevchenko A, Poulsen N & Kröger N (2022) Shedding light on silica biomineralization by comparative analysis of the silica‐associated proteomes from three diatom species. <i>The Plant Journal</i>, 110 (6), pp. 1700-1716.
Abstract: 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.
DOI Link: 10.1111/tpj.15765
Rights: This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
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