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  Self-Assembly of Highly Phosphorylated Silaffins and Their Function in Biosilica Morphogenesis

Kröger, N., Lorenz, S., Brunner, E., & Sumper, M. (2002). Self-Assembly of Highly Phosphorylated Silaffins and Their Function in Biosilica Morphogenesis. Science, 298(5593), 584-586. doi:10.1126/science.1076221.

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Kröger, Nils, Author
Lorenz, Sonja1, 2, Author                 
Brunner, Eike, Author
Sumper, Manfred, Author
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1Research Group Ubiquitin Signaling Specificity, MPI for Biophysical Chemistry, Max Planck Society, ou_3337583              
2External Organizations, ou_persistent22              

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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.

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Language(s): eng - English
 Dates: 2002-10-18
 Publication Status: Issued
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 Rev. Type: Peer
 Identifiers: DOI: 10.1126/science.1076221
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Title: Science
  Abbreviation : Science
Source Genre: Journal
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Publ. Info: Washington, D.C. : American Association for the Advancement of Science
Pages: - Volume / Issue: 298 (5593) Sequence Number: - Start / End Page: 584 - 586 Identifier: ISSN: 0036-8075
CoNE: https://pure.mpg.de/cone/journals/resource/991042748276600_1