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《Science of Sericulture》 2010-06
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Identification and Bioinformatic Analysis of a Parthenogenesis Associated Protein Phosphatidylinositol Glycan in Bombyx mori

ZHANG Wen-Ping L Zheng-Bing LONG Xiao-Hui NIE Zuo-Ming XIA Jia-Yin ZHANG Yao-Zhou(Institute of Biochemistry,School of Life Science,Zhejiang Sci-Tech University,Hangzhou 310018,China)  
Two-dimension gel electrophoresis (2DE) technique was used to identify differential protein spots between Bombyx mori eggs from normal sexual reproduction and those from parthenogenetic reproduction.After these protein spots were analyzed by MALDI-TOF-TOF MS,a large number of short peptide sequences were obtained.Alignments with sequences in a constructed cDNA library and in predicted protein database of Bombyx mori led to the identification of a phosphatidylinositol glycan protein (PGL) of which expression was up-regulated significantly in the process of parthenogenesis.In order to elucidate the function of PGL protein in Bombyx mori parthenogenesis,the full-length PGL protein gene was obtained by means of 5'-RACE.Bioinformatic analysis showed that this gene contains 1 038 nucleotides and encodes 345 amino acids with a predicted molecular weight of 39.516 kD and pI of 5.845.Moreover,the encoded protein harbors a conserved domain GPI8.Prediction of signal peptide showed that the probability of signal peptide was 0.997,suggesting its identity as a secreted protein.Functional domain prediction indicated that the protein has various functional sites including casein kinase Ⅱ phosphorylation,N-glycosylation,and protein kinase C phosphorylation sites.According to PGL protein's physical and chemical properties and its structural and functional domains,it is suggested that PGL protein participates in the process of Bombyx mori parthenogenesis and plays important roles in it through cell signaling pathway.
【Fund】: 国家自然科学基金项目(No.30277056);; 浙江省教育厅项目(No.Y201019098);; 浙江省生物医学工程重中之重学科开放基金项目(No.SWYX0915)
【CateGory Index】: S881.2
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