Long-range periodic sequence of the cement/silk protein of Stenopsyche marmorata: purification and biochemical characterisation.

The long-range periodic amino acid sequence of the bifunctional silk/cement protein from larvae of the caddisfly, Stenopsyche marmorata, is discussed in this study. The protein, named the S. marmorata silk protein (Smsp-1), was first purified to electrophoretic homogeneity. The results of Edman-based sequencing of Smsp-1 tryptic digests were consistent with the amino acid sequence deduced from a cDNA clone of the Smsp-1 gene. All undetected amino acids in the Edman-based sequencing were encoded as Ser, suggesting the presence of O-phospho-Ser. (31)P-NMR and an O-phospho-amino acid analysis successfully showed that the O-phospho-Ser residue occurred in a clustered manner, serving a cement function for Smsp-1. Two patterns of non-phosphorylated repeats, -SLGPYGDPRGDXLGPYGG- (X = V, G or D) and -GVGPYGDGLGPYGG-, were enriched in Smsp-1 compared with the O-phospho-Ser cluster, and have fibre-forming functions.