Characterization of a 200‐kDa Diatom Protein that is Specifically Associated with a Silica‐Based Substructure of the Cell Wall
- 1 November 1997
- journal article
- Published by Wiley in European Journal of Biochemistry
- Vol. 250 (1) , 99-105
- https://doi.org/10.1111/j.1432-1033.1997.00099.x
Abstract
The cell wall of a diatom is made up of a silica‐based scaffold and organic macromolecules. Proteins located in the cell wall are believed to control morphogenesis of the species‐specific silica structures of the scaffold. However, data that correlate distinct silica elements and specific proteins within the diatom cell wall have not been reported. Here, the cell wall protein HEP200 (200‐kDa HF‐extractable protein) from the diatom Cylindrotheca fusiformis is identified and characterized. HEP200 is tightly associated with a substructure of the silica scaffold. It is a member of a new protein family, of which two more members are identified. Each member displays the same bipartite structure. The N‐terminal part consists of a variable number of a repeated sequence motif (PSCD domain), whereas the C‐terminal part is unique. Immunolocalization experiments revealed the arrangement of different proteins within the cell wall. Frustulins, a previously described group of glycoproteins, constitute the outer coat of the cell wall and exhibit a ubiquitous distribution. In contrast, HEP200 is specifically located at a subset of about six silica strips in intact cell walls, shielded by frustulins. This study therefore identifies a diatom cell wall protein (HEP200) that is associated with a distinct substructure of the silica scaffold.Keywords
This publication has 20 references indexed in Scilit:
- Chapter 9 N-Glycosylation of Plant ProteinsNew Comprehensive Biochemistry, 1995
- [6] Use of T7 RNA polymerase to direct expression of cloned genesPublished by Elsevier ,1990
- The extracellular matrix of Volvox carteri: molecular structure of the cellular compartment.The Journal of cell biology, 1989
- A phosphodiester bridge between two arabinose residues as a structural element of an extracellular glycöprotein of Volvox carteriEuropean Journal of Biochemistry, 1989
- How do diatoms make silicon biominerals?Trends in Biochemical Sciences, 1987
- SDS—PAGE strongly overestimates the molecular masses of the neurofilament proteinsFEBS Letters, 1984
- Anhydrous hydrogen fluoride deglycosylates glycoproteinsAnalytical Biochemistry, 1977
- STUDIES ON THE BIOCHEMISTRY AND FINE STRUCTURE OF SILICA SHELL FORMATION IN DIATOMSThe Journal of cell biology, 1965
- Deposition of silica inside a diatom cellExperimental Cell Research, 1964