Abstract
Lepidopteran insects produce and secrete silk proteins mainly for cocoon formation. The lepidopteran silks generally consist of several components. Fibroins are a major component of the silks. So far as we know, two different types of fibroins have been described for the silk fiber construction. One is known in the saturniid silkmoth, wherein only one component, fibroin, forms homodimers with a disulfide bond and representing a unit of silk fiber formation (Tamura T, Inoue H, Suzuki Y, Mol Gen Genet 206:189–195, 1987; Tanaka K, Mizuno S, Insect Biochem Mol Biol 31:665–677, 2001). The other mode of fiber construction is the fibroin complex that consists of three components, that is, the fibroin heavy chain (fhc; about 350 kDa), the fibroin light chain (flc; 26 kDa) and P25 (or fibrohexamerin) (about 30 kDa) (Tanaka K, Mori K, Mizuno S, Biochem (Tokyo) 114:1–4, 1993, Tanaka K, Inoue S, Mizuno S, Insect Biochem Mol Biol 29:269–276, 1999a). The representative of this mode is that of Bombyx mori.
We present specific features of lepidopteran fibroins by highlighting Antheraea and Bombyx fibroins. Particularly, the two types of fibroins consist of different mode of repetitive structures. We describe details of these features. In addition, we illustrate structure and conformation for other lepidopteran and trichopteran fibroin system. As Trichoptera is the sister order of Lepidoptera, it is very interesting to compare them from the viewpoint of the evolution of silk proteins. Finally, we discuss mode of fibroin evolution.
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References
Chaitanya RK, Sridevi P, Senthilkumaran B, Gupta AD (2011) 20-Hydroxyecdysone regulation of H-fibroin gene in the stored grain pest Corcyra cephalonica, during the last instar larval development. Steroids 76:125–134
Chevillard M, Couble P, Prudhomme JC (1986) Complete nucleotide sequence of the gene encoding the Bombyx mori silkprotein P25 and predicted amino acid sequence of the protein. Nucleic Acids Res 14:6341–6342
Collin MA, Mita K, Sehnal F, Hayashi CY (2010) Molecular evolution of lepidopteran silk proteins: insights from the ghost moth, Hepialus californicus. J Mol Evol 70:519–529
Datta A, Ghosh AK, Kundu SC (2001) Differential expression of the fibroin gene in developmental stages of silkworm, Antheraea mylitta (Saturniidae). Comp Biochem Physiol B 129:197–204
Fedič R, Žurovec M, Sehnal F (2003) Correlation between fibroin amino acid sequence and physical silk properties. J Biol Chem 278:35255–35264
Fraser RDB, MacRae TP (1973) Conformation in fibrous proteins and related synthetic polypeptide. Academic, San Diego
Friedlander TP, Horst KR, Regier JC, Mitter C, Peigler RS, Fang QQ (1998) Two nuclear genes yield concordant relationships within Attacini (Lepidoptera: Saturniidae). Mol Phylogenet Evol 9:131–140
Hwang J-S, Lee J-S, Goo T-W, Yun E-Y, Lee K-S, Kim Y-S, Jin B-R, Lee S-M, Kim KL-Y, Kang S-W, Suh D-S (2001) Cloning of the fibroin gene from the oak silkworm, Antheraea yamamai and its complete sequence. Biotechnol Lett 23:1321–1326
Hynes RO (1987) Integrins: a family of cell surface receptors. Cell 48:549–554
Inoue S, Tanaka K, Arisaka F, Kimura S, Ohtomo K, Mizuno S (2000) Silk fibroin of Bombyx mori is secreted, assembling a high molecular mass elementary unit consisting of H-chain, L-chain, and P25, with a 6:6:1 molar ratio. J Biol Chem 275:40517–40528
Kikuchi Y, Mori K, Suzuki S, Yamaguchi K, Mizuno S (1992) Structure of the Bombyx mori fibroin light-chain-encoding gene: upstream sequence elements common to the light and heavy chain. Gene 110:151–158
Kirimura J (1962) Studies on amino acid composition and chemical structure of silk protein by microbiological determination. Bull Sericul Exp Sta 17:447–522 (in Japanese)
Kristensen NP (1975) The phylogeny of hexapod “orders”. A critical review of recent accounts. Zeitshrift für Zoologische Systematik und Evolutionsforschung 13:1–44
Kristensen NP (1991) Phylogeny of extant hexapods. In: Naumann ID (ed) The insects of Australia; a text for students and research workers, vol 1, 2nd edn. Cornell University Press, Ithaca, pp 125–140
Lam ST, Stahl MM, McMilin KD, Stahl FW (1974) Rec-mediated recombinational hot spot activity in bacteriophage lambda II: a mutation which causes hot spot activity. Genetics 77:425–433
Maning RF, Gage LP (1980) Internal structure of the silk fibroin gene of Bombyx mori II. Remarkable polymorphism of the organisation of crystalline and amorphus coding sequences. J Biol Chem 255:9451–9457
Mori K, Tanaka K, Kikuchi Y, Waga M, Waga S, Mizuno S (1995) Production of a chimeric fibroin light-chain polypeptide in a fibroin secretion-deficient naked pupa mutant of the silkworm Bombyx mori. J Mol Biol 251:217–228
Sehnal F, Sutherland T (2008) Silks produced by insect labial glands. Prion 2:145–153
Sehnal F, Žurovec M (2004) Construction of silk fiber core in Lepidoptera. Biomacromolecules 5:666–667
Sezutsu H, Yukuhiro K (2000) Dynamic rearrangement within the Antheraea pernyi silk fibroin gene is associated with four types of repetitive units. J Mol Evol 51:329–338
Sezutsu H, Tamura T, Yukuhiro K (2008a) Leucine-rich fibroin gene of the Japanese wild silkmoth, Rhodinia fugax Lepidoptera (Saturniidae). Eur J Entomol 105:561–566
Sezutsu H, Tamura T, Yukuhiro K (2008b) Uniform size of leucine-rich repeats in a wild silk moth Saturnia japonica (Lepidoptera Saturniidae) fibroin. Int J Wild Silkmoth Silk 13:53–60
Sezutsu H, Uchino K, Kobayashi I, Tamura T, Yukuhiro K (2010) Extensive sequence rearrangements and length polymorphism in fibroin genes in the wild silkmoth, Antheraea yamamai (Lepidoptera, Saturniidae). Int J Wild Silkmoth Silk 15:35–50
Takei F, Kikuchi Y, Kikuchi A, Mizuno S, Shimura K (1987) Further evidence for importance of the subunit combination of silkfibroin in its efficient secretion from the posterior silk gland cells. J Cell Biol 105:175–180
Tamura T, Kubota T (1989) A determination of molecular weight of fibroin polypeptides in the saturniid silkworms, Antheraea yamamai, Antheraea pernyi and Philosamia cynthia ricini by SDS PAGE. In: Akai H, Wu ZS (eds) Wild silkmoth ’88. International Society for Wild Silkmoths, Tokyo, pp 67–72
Tamura T, Inoue H, Suzuki Y (1987) The fibroin genes of the Antheraea yamamai and Bombyx mori are different in the core regions but reveal a striking sequences similarity in their 5′-ends and 5′-flanking regions. Mol Gen Genet 206:189–195
Tamura K, Peterson D, Peterson N, Stecher G, Nei M, Kumar S (2011) MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods. Mol Biol Evol 28:2731–2739
Tanaka K, Mizuno S (2001) Homologues of fibroin L-chain and P25 of Bombyx mori are present in Dendrolimus spectabilis and Papilio xuthus but not detectable in Antheraea yamamai. Insect Biochem Mol Biol 31:665–677
Tanaka K, Mori K, Mizuno S (1993) Immunological identification of the major disulfide-linked light component of silk fibroin. Biochem (Tokyo) 114:1–4
Tanaka K, Inoue S, Mizuno S (1999a) Hydrophobic interaction of P25, containing Asn-linked oligosaccharide chains, with the H–L complex of silk fibroin produced by Bombyx mori. Insect Biochem Mol Biol 29:269–276
Tanaka K, Kajiyama N, Ishikura K, Waga S, Kikuchi A, Ohtomo K, Takagi T, Mizuno S (1999b) Determination of the site of disulfide linkage between heavy and light chains of silkfibroin produced by Bombyx mori. Biochim Biophys Acta 1432:92–103
Thompson JD, Higgins DG, Gibson TJ (1997) CLUSTALW: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22:4673–4680
Tsujimoto Y, Suzuki Y (1979) The DNA sequence of Bombyx mori fibroin gene including the 5′ flanking, mRNA coding, entire intervening and fibroin protein coding regions. Cell 18:591–600
Wheeler WC, Whiting M, Wheeler QD, Carpenter JM (2001) The phylogeny of the extant hexapod orders. Cladistics 17:113–169
Whelan S, Goldman N (2001) A general empirical model of protein evolution derived from multiple protein families using a maximum-likelihood approach. Mol Biol Evol 18:691–699
Whiiting MF (2002) Phylogeny of the holometabolous insect orders: molecular evidence. Zool Scripta 31:3–15
Yamaguchi K, Kikuchi Y, Takagi T, Kikuchi A, Oyama F, Shimura K, Mizuno S (1989) Primary structure of the silk fibroin light chain determined by cDNA sequencing and peptide analysis. J Mol Biol 210:127–139
Yonemura N, Sehnal F (2006) The design of silk fiber composition in moths has been conserved for more than 150 million years. J Mol Evol 63:42–53
Yonemura N, Sehnal F, Mita K, Tamura T (2006) Protein composition of silk filaments spun under water by caddisfly larvae. Biomacromolecules 7:3370–3378
Yonemura N, Mita K, Tamura T, Sehnal F (2009) Conservation of silk genes in Trichoptera and Lepidoptera. J Mol Evol 68:641–653
Yukuhiro K, Kanda T, Tamura T (1997) Preferential codon usage and two types of repetitive motifs in the fibroin gene of the Chinese oak silkworm, Antheraea pernyi. Insect Mol Biol 6:89–95
Zhou C-Z, Confalonieri F, Medina N, Zivanovic Y, Esnault C, Yang T, Jacquet M, Janin J, Duguet M, Perasso R, Li Z-G (2000) Fine organization of Bombyx mori fibroin heavy chain gene. Nucleic Acid Res 28:2413–2419
Zhou C-Z, Confalonieri F, Jacquet M, Perasso R, Li Z-G, Janin J (2001) Silk fibroin: structural implications of a remarkable amino acid sequence. Proteins 44:119–122
Žurovec M, Sehnal F (2002) Unique molecular architecture of silkfibroin in the waxmoth, Galleria mellonella. J Biol Chem 277:22639–22647
Acknowledgment
We thank Prof. Tetsuo Asakura for his encouragement. We also express our thanks to Prof. Thomas A. Miller for his advice for improving our English writing. We thank Prof. František Sehnal for his critical reading and comments and for his discussion and guidance to Naoyuki Yonemura. We also appreciate Dr. Toshiki Tamura for their discussion and guidance to Naoyuki Yonemura.
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Yukuhiro, K., Sezutsu, H., Yonemura, N. (2014). Evolutionary Divergence of Lepidopteran and Trichopteran Fibroins. In: Asakura, T., Miller, T. (eds) Biotechnology of Silk. Biologically-Inspired Systems, vol 5. Springer, Dordrecht. https://doi.org/10.1007/978-94-007-7119-2_2
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DOI: https://doi.org/10.1007/978-94-007-7119-2_2
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