msmeg_2731, an uncharacterized nucleic acid binding protein from mycobacterium smegmatis, physically interacts with rps1msmeg_2731,但一个个从smegmatis分枝杆菌核酸结合蛋白,身体与rps1交互.pdfVIP

msmeg_2731, an uncharacterized nucleic acid binding protein from mycobacterium smegmatis, physically interacts with rps1msmeg_2731,但一个个从smegmatis分枝杆菌核酸结合蛋白,身体与rps1交互.pdf

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msmeg_2731, an uncharacterized nucleic acid binding protein from mycobacterium smegmatis, physically interacts with rps1msmeg_2731,但一个个从smegmatis分枝杆菌核酸结合蛋白,身体与rps1交互

MSMEG_2731, an Uncharacterized Nucleic Acid Binding Protein from Mycobacterium smegmatis, Physically Interacts with RPS1 1,3 1 1 1 1 1 Mingzhang Yang , Yuanyuan Chen , Ying Zhou , Liwei Wang , Hongtai Zhang , Li-Jun Bi *, Xian- En Zhang2* 1 Key Laboratory of Non-coding RNA, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China, 2 State Key Laboratory of Virology, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan, China, 3 Graduate School, Chinese Academy of Sciences, Beijing, China Abstract While the M. smegmatis genome has been sequenced, only a small portion of the genes have been characterized experimentally. Here, we purify and characterize MSMEG_2731, a conserved hypothetical alanine and arginine rich M. smegmatis protein. Using ultracentrifugation, we show that MSMEG_2731 is a monomer in vitro. MSMEG_2731 exists at a steady level throughout the M. smegmatis life-cycle. Combining results from pull-down techniques and LS-MS/MS, we show that MSMEG_2731 interacts with ribosomal protein S1. The existence of this interaction was confirmed by co- immunoprecipitation. We also show that MSMEG_2731 can bind ssDNA, dsDNA and RNA in vitro. Based on the interactions of MSMEG_2731 with RPS1 and RNA, we propose that MSMEG_2731 is involved in the transcription-translation process in vivo. Citation: Yang M, Chen Y, Zhou Y, Wang L, Zhang H, et al. (2012) MSMEG_2731, an Uncharacterized Nucleic Acid Binding Protein from Mycobacterium smegmatis, Physically Interacts with RPS1. PLoS ONE 7(5): e36666. doi:10.1371/journal.pone.0036666 Editor: Bostjan Kobe, University of Queensland, Australia Received July 22, 2011; Accepted April 4,

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