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Recognition of signal peptide by protein translocation machinery in middle silk gland of silkworm Bombyx mori

Guo, X. ; Zhang, Y. ; Zhang, X. ; Wang, S. ; Lu, C.

Acta Biochimica et Biophysica Sinica, 01/01/2008, Vol.40(1), pp.38-46 [Tạp chí có phản biện]

ISSN: 1672-9145 ; E-ISSN: 1745-7270 ; DOI: http://dx.doi.org/10.1111/j.1745-7270.2008.00376.x

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  • Nhan đề:
    Recognition of signal peptide by protein translocation machinery in middle silk gland of silkworm Bombyx mori
  • Tác giả: Guo, X. ; Zhang, Y. ; Zhang, X. ; Wang, S. ; Lu, C.
  • Chủ đề: Biology
  • Là 1 phần của: Acta Biochimica et Biophysica Sinica, 01/01/2008, Vol.40(1), pp.38-46
  • Mô tả: To investigate the functions of signal peptide in protein secretion in the middle silk gland of silkworm Bombyx mori, a series of recombinant Autographa californica multiple nucleopolyhedroviruses containing enhanced green fluorescent protein (egfp) gene, led by sericin-1 promoter and mutated signal peptide coding sequences, were constructed by region-deletions or single amino acid residue deletions. The recombinant Autographa californica multiple nucleopolyhedroviruses were injected into the hemocoele of newly ecdysed fifth-instar silkworm larvae. The expression and secretion of EGFP in the middle silk gland were examined by fluorescence microscopy and Western blot analysis. Results showed that even with a large part (up to 14 amino acid residues) of the ser-1 signal peptide deleted, the expressed EGFP could still be secreted into the cavity of the silk gland. Western blot analysis showed that shortening of the signal peptide from the C-terminal suppressed the maturation of pro-EGFP to EGFP. When 8 amino acid residues were deleted from the C-terminal of the signal peptide (mutant 13 aa), the secretion of EGFP was incomplete, implicating the importance of proper coupling of the h-region and c-region. The deletion of amino acid residue(s) in the h-region did not affect the secretion of EGFP, indicating that the recognition of signal peptide by translocation machinery was mainly by a structural domain, but not by special amino acid residue(s). Furthermore, the deletion of Arg2 or replacement with Asp in the n-region of the signal peptide did not influence secretion of EGFP, suggesting that a positive charge is not crucial.
  • Ngôn ngữ: English
  • Số nhận dạng: ISSN: 1672-9145 ; E-ISSN: 1745-7270 ; DOI: http://dx.doi.org/10.1111/j.1745-7270.2008.00376.x

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