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Journal of Biochemistry 2005 138(5):593-604; doi:10.1093/jb/mvi155
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© 2005 The Japanese Biochemical Society

Regular Paper

Unique Molecular Architecture of Egg Case Silk Protein in a Spider, Nephila clavata

Aichun Zhao1, Tianfu Zhao1, Yanghu SiMa2, Yuansong Zhang1, Koichi Nakagaki1, Yungen Miao3, Kunihiro Shiomi1, Zenta Kajiura1, Yoko Nagata4 and Masao Nakagaki1,*

1 Department of Applied Biology, Faculty of Textile Science and Technology, Shinshu University, Ueda 386-8567; 2 Faculty of Agricultural Science and Technology, Suzhou University, Su Zhou 215006, China; 3 College of Animal Sciences, Zhejiang University, Hang Zhou 310029, China; and 4 College of Science and Technology, Nihon University, Tokyo 101-8308

* To whom correspondence should be addressed. Tel: +81-268-21-5335, Fax: +81-268-21-5331; E-mail: nakagak{at}giptc.shinshu-u.ac.jp

We describe a unique silk protein secreted from the cylindrical silk glands of the spider Nephila clavata. This silk is primarily composed of three proteins, whose transcripts of approximately 16.0, 14.5 and 13.0 kb are homologous to one another in two termini and repetitive units, as determined on Northern blotting. Its overall organization shows that it is similar to other characterized silk proteins, including in the mainly central repetitive region as well as the non-repetitive N-terminal (166 residues) and C-terminal (176 residues) parts. However, up to 90% of the protein consists of highly ordered repetitive structures that are not found in other silks. The repetitive region mainly consists of several types of complexes and remarkably conserved polypeptide repeats. The assembled repeat units (A1B1) contain a high proportion of Ala (30.41%), Ser (25.15%), and residues with hydrophobic side chains (22.22% for Gly, Leu, Ile, Val and Phe combined). The presence of Ser-rich and GVGAGASA motifs suggests the formation of a ß-sheet. The repetitive region is characterized by alternating arrays of hydrophobic and hydrophilic blocks. The results suggested that this egg case silk is an exceptional protein when compared with previously investigated spider silks.


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