| 腾冲嗜热菌单链 DNA 结合蛋白 SSB2 和 SSB3 新的单链 DNA 结合特性 |
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| 引用本文： | 张树利,杨海花,李磊,田宇清,谭华荣.腾冲嗜热菌单链 DNA 结合蛋白 SSB2 和 SSB3 新的单链 DNA 结合特性[J].微生物学报,2009,49(4):453-459. |
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| 作者姓名： | 张树利 杨海花 李磊 田宇清 谭华荣 |
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| 作者单位： | 1. 中国科学院微生物研究所,北京100101;中国科学院研究生院,北京100039
2. 中国科学院微生物研究所,北京,100101 |
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| 基金项目： | 国家自然科学基金(30621005) 和国家高技术研究发展计划 (2009CB118905) |
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| 摘 要： | 摘要：【目的】揭示腾冲嗜热菌中两个单链DNA结合蛋白SSB2和SSB3的全新的底物结合功能及其不同的体内表达模式。【方法】利用腾冲嗜热菌复制起始位点附近的长度较短的单链DNA为底物，采用非变性聚丙烯酰胺凝胶电泳及western blot方法，研究SSB2和SSB3体外单链DNA结合特征和体内表达模式。【结果】SSB2 与35nt的复制起始区单链DNA（ssDNA）结合, 形成单个SSB2-DNA复合物；当与59 nt ssDNA结合时，可以随着蛋白浓度的递增形成一个或两个SSB2-DNA复合物；而与70n
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| 关 键 词： | 关键词：单链DNA结合蛋白 蛋白构型 蛋白表达模式 |
| 收稿时间： | 2008/2/11 0:00:00 |
Novel ssDNA-binding properties of SSB2 and SSB3 from Thermoanaerobacter tengcongensis |
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| Shuli Zhang,Haihua Yang,Lei Li,Yuqing Tian and Huarong Tan.Novel ssDNA-binding properties of SSB2 and SSB3 from Thermoanaerobacter tengcongensis[J].Acta Microbiologica Sinica,2009,49(4):453-459. |
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| Authors: | Shuli Zhang Haihua Yang Lei Li Yuqing Tian and Huarong Tan |
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| Institution: | State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China;State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China;State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China;State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China;State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China |
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| Abstract: | Objective] SSB2 and SSB3 are ssDNA-binding proteins of Thermoanaerobacter tengcongensis. This work aimed to disclose novel properties of both proteins. Methods ] We performed electrophorefic mobility shift assays (EMSAs) using oligonucleotides spanning the replication origin of T. tengcongensis and non-denaturing polyacrylamide gels. Western blotting assays were used to study the expression patterns of both proteins. Results] SSB2 bound to 35-nt, 59-nt and 70-nt ssDNA spanning the replication origin and formed one, two or three DNA-protein consplexes. The number of the SSB2-DNA complexes was determined by both the length of the ssDNA and the concentration of SSB2. SSB3 formed one more DNA-protein complex with 59-nt or 70-nt ssDNA in comparison with SSB2. Storage of the proteins at - 70℃led to the disappearance of one SSB2-(70-nt) complex, or two SSB3-(59-nt) complexes or three SSB3-(70-nt) complexes in the EMSA,indicating the distinct loss of the SSBs's conformations. Moreover,SSB2 and SSB3 displayed different expression patterns at variable incubation temperatures in vivo. Conclusion ] SSB2 and SSB3 could bind ssDNA with various conformations that were determined by the length of ssDNA, the concentration of the proteins, as well as the tempe~ture of treatment. To our knowledge, this is the fast disclosure of the characteristics of SSB2 and SSB3 on 35-70 nt oligonucleotides. |
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| Keywords: | Single-stranded binding protein (SSB) ssDNA-binding profile protein conformation protein expression pattern |
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