N. Kroger et al., FRUSTULINS - DOMAIN CONSERVATION IN A PROTEIN FAMILY ASSOCIATED WITH DIATOM CELL-WALLS, European journal of biochemistry, 239(2), 1996, pp. 259-264
The outstanding feature of a diatom is the species-specific design and
ornamentation of the silica-based cell wall, termed frustulum. A new
frustulum is shaped in a specialized organelle (silica deposition vesi
cle) and secreted. Proteins in the lumen of this organelle may control
the biomineralization process and are likely to remain associated wit
h the mature cell wall. Therefore a study of the structures of protein
s associated with the diatom cell wall was initiated. The complete pri
mary structures of three cell wall proteins (denoted as frustulins) ha
ve been determined. In addition, partial amino acid sequences from two
more cell wall components were obtained. From these data, a highly co
nserved domain has been identified as a common building block of diato
m cell wall proteins that is repeated several times per polypeptide ch
ain together with polyproline/hydroxyproline or polyglycine spacers. A
ll frustulins characterized so far, are synthesized as preproteins wit
h a novel type of N-terminal presequence.