Recognition of signal peptide by protein translocation machinery in middle silk gland of silkworm Bombyx mori
文献类型：期刊论文
| 作者 | Guo, XY; Zhang, Y; Zhang, X; Wang, SP; Lu, CD |
| 刊名 | ACTA BIOCHIMICA ET BIOPHYSICA SINICA
 |
| 出版日期 | 2008 |
| 卷号 | 40期号:1页码:38-46 |
| 关键词 | signal peptide recognition sericin-1 silkworm Bombyx mori recombinant AcMNPV |
| 通讯作者 | Lu, C (reprint author), Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Biochem & Cell Biol, State Key Lab Mol Biochem, Shanghai 200031, Peoples R China.,cdlu@sibs.ac.cn |
| 英文摘要 | 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 Arg(2) 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. |
| 学科主题 | Biochemistry & Molecular Biology; Biophysics |
| 类目[WOS] | Biochemistry & Molecular Biology ; Biophysics |
| 关键词[WOS] | ENDOPLASMIC-RETICULUM MEMBRANE ; SEQUENCE RECOGNITION ; PARTICLE RECEPTOR ; CLEAVAGE SITE ; BETA-SUBUNIT ; GENE ; ORGANIZATION ; TRANSPORT ; COMPLEX ; REGION |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000252423900005 |
| 版本 | 出版稿 |
| 源URL | [http://202.127.25.143/handle/331003/1322]  |
| 专题 | 上海生化细胞研究所_上海生科院生化细胞研究所 |
| 推荐引用方式 GB/T 7714 | Guo, XY,Zhang, Y,Zhang, X,et al. Recognition of signal peptide by protein translocation machinery in middle silk gland of silkworm Bombyx mori[J]. ACTA BIOCHIMICA ET BIOPHYSICA SINICA,2008,40(1):38-46. |
| APA | Guo, XY,Zhang, Y,Zhang, X,Wang, SP,&Lu, CD.(2008).Recognition of signal peptide by protein translocation machinery in middle silk gland of silkworm Bombyx mori.ACTA BIOCHIMICA ET BIOPHYSICA SINICA,40(1),38-46. |
| MLA | Guo, XY,et al."Recognition of signal peptide by protein translocation machinery in middle silk gland of silkworm Bombyx mori".ACTA BIOCHIMICA ET BIOPHYSICA SINICA 40.1(2008):38-46. |
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