- AutorIn
- Alastair W. Skeffington Max-Planck-Institute of Molecular Plant Physiology Potsadam#B CUBE Center for Molecular Bioengineering, TU Dresden
- Marc GentzelCenter for Cellular and Molecular Bioengineering, TU Dresden
- Andre OharaB CUBE Center for Molecular Bioengineering, TU Dresden
- Alexander Milentyev
- Christoph Heintze
- Lorenz Böttcher
- Stefan Görlich
- Andrej Shevchenko
- Nicole Poulsen
- Nils Kröger
- Titel
- Shedding light on silica biomineralization by comparative analysis of the silica-associated proteomes from three diatom species
- Zitierfähige Url:
- https://nbn-resolving.org/urn:nbn:de:bsz:14-qucosa2-906195
- Quellenangabe
- The plant journal
Erscheinungsjahr: 2022
Jahrgang: 110
Heft: 6
Seiten: 1700-1716
E-ISSN: 1365-313X - Erstveröffentlichung
- 2022
- Abstract (EN)
- 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.
- Andere Ausgabe
- Link zum Artikel der zuerst in der Zeitschrift „The plant journal” bei Wiley erschienen ist.
DOI: 10.1111/tpj.15765 - Freie Schlagwörter (DE)
- Biokieselsäure, Morphogenese der Kieselsäure, intrinsisch ungeordnete Proteine, Silaffine, GFP-Tagging, Kegelstumpf, Fultoportula, Thalassiosira pseudonana, Thalassiosira oceanica und Cyclotella cryptica
- Freie Schlagwörter (EN)
- biosilica, silica morphogenesis, intrinsically disordered proteins, silaffins, GFP-tagging, frustule, fultoportula, Thalassiosira pseudonana, Thalassiosira oceanica and Cyclotella cryptica
- Klassifikation (DDC)
- 580
- Verlag
- Wiley-Blackwell, Oxford [u.a.]
- Förder- / Projektangaben
- Deutsche Forschungsgemeinschaft (DFG)
FOR 2038: Die Rolle nanostrukturierter organischer Matrizen in der biologischen Mineralisation des Silica
ID: 233120155 - Bundesministerium für Bildung und Forschung (BMBF)
Strategische Investitionen für Einrichtung und Ausbau der Technologieplattformen des ZIK B CUBE
ID: 03Z22EB1 - Deutsche Forschungsgemeinschaft (DFG)
ID: KR 1852/8-2 - Deutsche Forschungsgemeinschaft (DFG)
ID: INST 269/731-1 - Deutsche Forschungsgemeinschaft (DFG)
ID: SH94/4-2 - Deutsche Forschungsgemeinschaft (DFG)
ID: SH94 - European Regional Development Fund (EFRE)
ID: 100232736 - Version / Begutachtungsstatus
- publizierte Version / Verlagsversion
- URN Qucosa
- urn:nbn:de:bsz:14-qucosa2-906195
- Veröffentlichungsdatum Qucosa
- 05.04.2024
- Dokumenttyp
- Artikel
- Sprache des Dokumentes
- Englisch
- Lizenz / Rechtehinweis
CC BY 4.0