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Aligning the proteome and genome of the silkworm, Bombyx mori
Authors:Yaozhou Zhang  Qingyou Xia  Jie Xu  Jian Chen  Zuoming Nie  Dan Wang  Wenping Zhang  Jianqing Chen  Qingliang Zheng  Qing Chen  Lingying Kong  Xiaoyuan Ren  Jiang Wang  Zhengbing Lv  Wei Yu  Caiying Jiang  Lili Liu  Qing Sheng  Yongfeng Jin  Xiangfu Wu
Affiliation:1. The Key Laboratory of Bioreactor and Biopharmacy of Zhejiang Province, Institute of Biochemistry, Zhejiang Sci-Tech University, Xiasha High-Tech Zone No.2 Road, Hangzhou, 310018, China
2. The Key Sericultural Laboratory of Agricultural Ministry, The Key Laboratory for Sericultural Sciences and Genomics of the Ministry of Education, College of Biotechnology, Southwest University, Beibei, Chongqing, 400715, China
3. College of Life Sciences, Zhejiang University, Hangzhou, 310029, China
Abstract:A technology of mass spectrometry (MS) was used in this study for the large-scale proteomic identification and verification of protein-encoding genes present in the silkworm (Bombyx mori) genome. Peptide sequences identified by MS were compared with those from an open reading frame (ORF) library of the B. mori genome and a cDNA library, to validate the coding attributes of ORFs. Two databases were created. The first was based on a 9× draft sequence of the silkworm genome and contained 14,632 putative proteins. The second was based on a B. mori pupal cDNA library containing 3,187 putative proteins of at least 30 amino acid residues in length. A total of 81,000 peptide sequences with a threshold score of 60% were generated by the MS/MS analysis, and 55,400 of these were chosen for a sequence alignment. By searching these two databases, 6,649 and 250 proteins were matched, which accounted for approximately 45.4% and 7.8% of the peptide sequences and putative proteins, respectively. Further analyses carried out by several bioinformatic tools suggested that the matches included proteins with predicted transmembrane domains (1,393) and preproteins with a signal peptide (976). These results provide a fundamental understanding of the expression and function of silkworm proteins.
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