From EST sequence to spider silk spinning: identification and molecular characterisation of Nephila senegalensis major ampullate gland peroxidase NsPox.
Spider dragline silk is renowned as one of the toughest materials of its kind. In nature, spider silks are spun out of aqueous solutions under environmental conditions. This is in contrast to production of most synthetic fibres, where hazardous solvents, high temperatures and pressure are used. In order to identify some of the chemical processes involved in spider silk spinning, we have produced a collection of cDNA sequences from specific regions of Nephila senegalensis major ampullate gland. We examined in detail the sequence and expression of a putative Nephila senegalensis peroxidase gene (NsPox) from our EST collection. NsPox encodes a protein with similarity to Drosophila melanogaster and Aedes aegypti peroxidases. Northern analysis and in situ localisation experiments revealed that NsPox is expressed in major and minor ampullate glands of the spider where the main components of the dragline silk are produced. We suggest that NsPox plays a role in dragline silk fibre formation and/or processing.
Pouchkina
N N
NN
Centre for Novel Agricultural Products, Department of Biology, University of York, York YO10 5YW, UK. nps2@york.ac.uk
Stanchev
B S
BS
McQueen-Mason
S J
SJ
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D018076:DNA, Complementary; D004331:Drosophila melanogaster / Q000201:enzymology / Q000235:genetics; D020224:Expressed Sequence Tags; D015723:Gene Library; D017403:In Situ Hybridization; D019476:Insect Proteins / Q000235:genetics*; D008969:Molecular Sequence Data; D010544:Peroxidases / Q000737:chemistry / Q000235:genetics*; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D047011:Silk; D013112:Spiders / Q000235:genetics / Q000502:physiology*
D018076:DNA, Complementary; D019476:Insect Proteins; D047011:Silk; D010544:Peroxidases