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Shape evolution with temperature of a thermotolerant protein (PeaT1) in solution detected by small angle X-ray scattering

Authors

  • Xueqing Xing,

    1. Beijing Synchrotron Radiation Facility, Institute of High Energy Physics, Chinese Academy of Sciences, Beijing 100049, People's Republic of China
    2. Graduate University of Chinese Academy of Sciences, Beijing 100049, People's Republic of China
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    • Xueqing Xing and Quan Liu contributed equally to this work.

  • Quan Liu,

    1. State Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing 100081, People's Republic of China
    2. College of Life Science and Technology, Heilongjiang Bayi Agricultural University, Daqing 163319, People's Republic of China
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    • Xueqing Xing and Quan Liu contributed equally to this work.

  • Wei Wang,

    1. Beijing Synchrotron Radiation Facility, Institute of High Energy Physics, Chinese Academy of Sciences, Beijing 100049, People's Republic of China
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  • Kunhao Zhang,

    1. Beijing Synchrotron Radiation Facility, Institute of High Energy Physics, Chinese Academy of Sciences, Beijing 100049, People's Republic of China
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  • Tang Li,

    1. State Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing 100081, People's Republic of China
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  • Quan Cai,

    1. Beijing Synchrotron Radiation Facility, Institute of High Energy Physics, Chinese Academy of Sciences, Beijing 100049, People's Republic of China
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  • Guang Mo,

    1. Beijing Synchrotron Radiation Facility, Institute of High Energy Physics, Chinese Academy of Sciences, Beijing 100049, People's Republic of China
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  • Weidong Cheng,

    1. Beijing Synchrotron Radiation Facility, Institute of High Energy Physics, Chinese Academy of Sciences, Beijing 100049, People's Republic of China
    2. Graduate University of Chinese Academy of Sciences, Beijing 100049, People's Republic of China
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  • Dehong Wang,

    1. Beijing Synchrotron Radiation Facility, Institute of High Energy Physics, Chinese Academy of Sciences, Beijing 100049, People's Republic of China
    2. Graduate University of Chinese Academy of Sciences, Beijing 100049, People's Republic of China
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  • Yu Gong,

    1. Beijing Synchrotron Radiation Facility, Institute of High Energy Physics, Chinese Academy of Sciences, Beijing 100049, People's Republic of China
    2. Graduate University of Chinese Academy of Sciences, Beijing 100049, People's Republic of China
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  • Zhongjun Chen,

    1. Beijing Synchrotron Radiation Facility, Institute of High Energy Physics, Chinese Academy of Sciences, Beijing 100049, People's Republic of China
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  • Dewen Qiu,

    Corresponding author
    1. State Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing 100081, People's Republic of China
    • State Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing 100081, People's Republic of China
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  • Zhonghua Wu

    Corresponding author
    1. Beijing Synchrotron Radiation Facility, Institute of High Energy Physics, Chinese Academy of Sciences, Beijing 100049, People's Republic of China
    2. Graduate University of Chinese Academy of Sciences, Beijing 100049, People's Republic of China
    • 19B Yuquan Road, Shijingshan District, Beijing 100049, Republic of China
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Abstract

The protein elicitor from Alternaria tenuissima (PeaT1) presented excellent thermotolerance and potential application in agriculture as a pesticide. Previous synchrotron radiation circular dichroism study demonstrated that the secondary structures in PeaT1 protein are reversible with temperature change. To further clarify the mechanism of its thermotolerance, synchrotron radiation small angle x-ray scattering (SAXS) technique was used to study the shape change of PeaT1 protein with temperature in this article. Ab initio structure restorations based on the SAXS data revealed that PeaT1 protein has a prolate shape with a P2 symmetry axis along the prolate anisometric direction. With temperature increase, a gooseneck vase-like (25°C), to jug-like (55°C), then to oval (85°C) shape change can be found, and these shape changes are also approximately reversible with temperature decrease. PeaT1 protein contains two homogenous molecules, and each of them consists of F, NAC, T, and UBA domains. The structures of the four domains were predicted. Simulated annealing algorithm was used to superimpose the domain structures onto the SAXS shapes. It was found that all the structural domains have position rotation and translation with temperature change, but the NAC domains are relatively stable, playing a role of frame. This shape change information provides clues for further exploring its biological function and application. Proteins 2013. © 2012 Wiley Periodicals, Inc.

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