identification and characterization of argonaute protein, ago2 and its associated small rnas in schistosoma japonicum识别和描述argonaute蛋白质,在日本血吸虫ago2及其相关的小分子rna.pdfVIP

identification and characterization of argonaute protein, ago2 and its associated small rnas in schistosoma japonicum识别和描述argonaute蛋白质,在日本血吸虫ago2及其相关的小分子rna.pdf

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identification and characterization of argonaute protein, ago2 and its associated small rnas in schistosoma japonicum识别和描述argonaute蛋白质,在日本血吸虫ago2及其相关的小分子rna

Identification and Characterization of Argonaute Protein, Ago2 and Its Associated Small RNAs in Schistosoma japonicum 1 1 1 1 2 1,3 Pengfei Cai , Xianyu Piao , Nan Hou , Shuai Liu , Heng Wang , Qijun Chen * 1 MOH Key Laboratory of Systems Biology of Pathogens, Institute of Pathogen Biology, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, People’s Republic of China, 2 Department of Microbiology and Parasitology, Institute of Basic Medical Sciences, Chinese Academy of Medical Sciences and School of Basic Medicine, Peking Union Medical College, Beijing, People’s Republic of China, 3 Key Laboratory of Zoonosis, Ministry of Education, Institute of Zoonosis, Jilin University, Changchun, People’s Republic of China Abstract Background: The complex life cycle of the genus Schistosoma drives the parasites to employ subtle developmentally dependent gene regulatory machineries. Small non-coding RNAs (sncRNAs) are essential gene regulatory factors that, through their impact on mRNA and genome stability, control stage-specific gene expression. Abundant sncRNAs have been identified in this genus. However, their functionally associated partners, Argonaute family proteins, which are the key components of the RNA-induced silencing complex (RISC), have not yet been fully explored. Methodology/Principal Findings: Two monoclonal antibodies (mAbs) specific to Schistosoma japonicum Argonaute protein Ago2 (SjAgo2), but not SjAgo1 and SjAgo3, were generated. Soluble adult worm antigen preparation (SWAP) was subjected to immunoprecipitation with the mAbs and the captured SjAgo2 protein was subsequently confirmed by Western blot and mass spectrometry (MS) analysis. The small RNA

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