Characterization of a 200-kDa diatom protein that is specifically associated with a silica-based substructure of the cell wall

被引:120
作者
Kroger, N [1 ]
Lehmann, G [1 ]
Rachel, R [1 ]
Sumper, M [1 ]
机构
[1] UNIV REGENSBURG,LEHRSTUHL MIKROBIOL,D-93040 REGENSBURG,GERMANY
来源
EUROPEAN JOURNAL OF BIOCHEMISTRY | 1997年 / 250卷 / 01期
关键词
biomineralization; Cylindrotheca fusiformis; girdle band; immunolocalization; morphogenesis;
D O I
10.1111/j.1432-1033.1997.00099.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 HEP2OO (200-kDa HE-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.
引用
收藏
页码:99 / 105
页数:7
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