Self-assembly of highly phosphorylated silaffins and their function in biosilica morphogenesis

Kroeger, Nils and Lorenz, Sonja and Brunner, Eike and Sumper, Manfred (2002) Self-assembly of highly phosphorylated silaffins and their function in biosilica morphogenesis. SCIENCE, 298 (5593). pp. 584-586. ISSN 0036-8075

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Abstract

Silaffins are uniquely modified peptides that have been implicated in the biogenesis of diatom biosilica. A method that avoids the harsh anhydrous hydrogen fluoride treatment commonly used to dissolve biosilica allows the extraction of silaffins in their native state. The native silaffins carry further posttranslational modifications in addition to their polyamine moieties. Each serine residue was phosphorylated, and this high level of phosphorylation is essential for biological activity. The zwitterionic structure of native silaffins enables the formation of supramolecular assemblies. Time-resolved analysis of silica morphogenesis in vitro detected a plastic silaffin-silica phase, which may represent a building material for diatom biosilica.

Item Type: Article
Uncontrolled Keywords: DIATOM BIOSILICA; SILICA; DEPOSITION; PROTEINS; PEPTIDES;
Subjects: 500 Science > 540 Chemistry & allied sciences
500 Science > 570 Life sciences
Divisions: Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Alumni or Retired > Prof. Dr. Eike Brunner
Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Alumni or Retired > Prof. Dr. Manfred Sumper
Depositing User: Dr. Gernot Deinzer
Date Deposited: 26 Aug 2021 14:53
Last Modified: 26 Aug 2021 14:53
URI: https://pred.uni-regensburg.de/id/eprint/39774

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