Structural analysis of fibroin heavy chain signal peptide of silkworm Bombyx mori

Acta Biochimica et Biophysica Sinica

Volumn 38, Issue 7, 2006, Pages 507-513

  Wang, Sheng Peng ^a,b   Guo, Ting Qing ^a   Guo, Xiu Yang ^a   Huang, Jun Ting ^b   Lu, Chang De ^a  

^a INSTITUTE OF BIOCHEMISTRY AND CELL BIOLOGY   (China)

^b INSTITUTE OF PLANT PROTECTION   (China)

Author keywords

Fibroin heavy chain; Racmnpv; Signal peptide; Silkworm, bombyx mori

Indexed keywords

ENHANCED GREEN FLUORESCENT PROTEIN; FIBROIN; FIBROIN, SILKWORM; GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; INSECT PROTEIN; SIGNAL PEPTIDE;

ANIMAL; ARTICLE; BACULOVIRUS; CHEMISTRY; GENETICS; ISOLATION AND PURIFICATION; PHYSIOLOGY; SECRETION; SEQUENCE ANALYSIS; SILKWORM;

ANIMALS; BACULOVIRIDAE; BOMBYX; FIBROINS; GREEN FLUORESCENT PROTEINS; INSECT PROTEINS; PROTEIN SORTING SIGNALS; RECOMBINANT FUSION PROTEINS; SEQUENCE ANALYSIS, PROTEIN;

BOMBYX MORI;

EID: 33746265199     PISSN: 16729145     EISSN: 17457270     Source Type: Journal    
DOI: 10.1111/j.1745-7270.2006.00189.x     Document Type: Article

References (22)

1. Walter P, Blobel G. Translocation of proteins across the endoplasmic reticulum III. Signal recognition protein (SRP) causes signal sequence-dependent and site-specific arrest of chain elongation that is released by microsomal membranes. J Cell Biol 1981, 91: 557-561
2. Gierasch LM. Signal sequences. Biochemistry 1989, 28: 923-930
3. von Heijne G. Patterns of amino acids near signal-sequence cleavage sites. Eur J Biochem 1983, 133: 17-21
4. von Heijne G. Signal sequences. The limits of variation. J Mol Biol 1985, 184: 99-105
5. von Heijne G. The signal peptide. J Membr Biol 1990, 115: 195-201
6. Guo TQ, Wang JY, Wang SP, Guo XY, Huang KW, Huang JT, Lu CD. Loss of posterior silk gland transcription specificity of fibroin light chain promoter due to absence of 41 bp sequence containing possible inhibitor binding sites. Acta Biochim Biophys Sin 2005, 37: 819-825
7. Inoue S, Tanaka K, Arisaka F, Kimura S, Ohtomo K, Mizuno S. 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 2000, 275: 40517-40528
8. Sasaki T, Noda H. Studies on silk fibroin of Bombyx mori directly extracted from the silk gland. III. N-terminal analysis and degradation in slightly alkaline solution. J Biochem (Tokyo) 1974, 76: 493-502
9. Zhou CZ, Confalonieri F, Medina N, Zivanovic Y, Esnault C, Yang T, Jacquet M et al. Fine organization of Bombyx mori fibroin heavy chain gene. Nucleic Acids Res 2000, 28: 2413-2419
10. Wang SP, Guo TQ, Quo XY, Huang JT, Lu CD. In vivo analysis of fibroin heavy chain signal peptide of silkworm Bombyx mori using recombinant baculovirus as vector. Biochem Biophys Res Commun 2006, 341: 1203-1210
11. Nielsen H, Engelbrecht J, Brunak S, von Heijne G. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng 1997, 10: 1-6
12. Bendtsen JD, Nielsen H, von Heijne G, Brunak S. Improved prediction of signal peptides: SignalP 3.0. J Mol Biol 2004, 340: 783-795
13. Guo TQ, Wang JY, Guo XY, Wang SP, Lu CD. Transient in vivo gene delivery to the silkworm Bombyx mori by EGT-null recombinant AcNPV using EGFP as a reporter. Arch Virol 2005, 150: 93-105
14. Guo XY, Guo TQ, Wang SP, Wang JY, Lu CD. Silk gland specific secretory expression of egfp gene in silkworm Bombyx mori with rAcMNPV system. Arch Virol 2005, 150: 1151-1160
15. Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227: 680-685
16. Matsudaira P. Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J Biol Chem 1987, 262: 10035-10038
17. Martoglio B, Dobberstein B. Signal sequences: More than just greasy peptides. Trends Cell Biol 1998, 8: 410-415
18. von Heijne G, Abrahmsen L. Species-specific variation in signal peptide design. Implications for protein secretion in foreign hosts. FEBS Lett 1989, 244: 439-446
19. Menne KM, Hermjakob H, Apweiler R. A comparison of signal sequence prediction methods using a test set of signal peptides. Bioinformatics 2000, 16: 741-742
20. Inoue S, Kanda T, Imamura M, Quan GX, Kojima K, Tanaka H, Tomita M et al. A fibroin secretion-deficient silkworm mutant, Nd-sD, provides an efficient system for producing recombinant proteins. Insect Biochem Mol Biol 2005, 35: 51-59
21. Royer C, Jalabert A, Da Rocha M, Grenier AM, Mauchamp B, Couble P, Chavancy G. Biosynthesis and cocoon-export of a recombinant globular protein in transgenic silkworms. Transgenic Res 2005, 14: 463-472
22. Tomita M, Munetsuna H, Sato T, Adachi T, Hino R, Hayashi M, Shimizu K et al. Transgenic silkworms produce recombinant human type III procollagen in cocoons. Nat Biotechnol 2003, 21: 52-56