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

  1. Xueqing Xing1,2,†,
  2. Quan Liu3,4,†,
  3. Wei Wang1,
  4. Kunhao Zhang1,
  5. Tang Li3,
  6. Quan Cai1,
  7. Guang Mo1,
  8. Weidong Cheng1,2,
  9. Dehong Wang1,2,
  10. Yu Gong1,2,
  11. Zhongjun Chen1,
  12. Dewen Qiu3,*,
  13. Zhonghua Wu1,2,*

Article first published online: 15 SEP 2012

DOI: 10.1002/prot.24162

Issue

Proteins: Structure, Function, and Bioinformatics

Proteins: Structure, Function, and Bioinformatics

Volume 81, Issue 1, pages 53–62, January 2013

Additional Information

How to Cite

Xing, X., Liu, Q., Wang, W., Zhang, K., Li, T., Cai, Q., Mo, G., Cheng, W., Wang, D., Gong, Y., Chen, Z., Qiu, D. and Wu, Z. (2013), Shape evolution with temperature of a thermotolerant protein (PeaT1) in solution detected by small angle X-ray scattering. Proteins, 81: 53–62. doi: 10.1002/prot.24162

Author Information

  1. 1

    Beijing Synchrotron Radiation Facility, Institute of High Energy Physics, Chinese Academy of Sciences, Beijing 100049, People's Republic of China

  2. 2

    Graduate University of Chinese Academy of Sciences, Beijing 100049, People's Republic of China

  3. 3

    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

  4. 4

    College of Life Science and Technology, Heilongjiang Bayi Agricultural University, Daqing 163319, People's Republic of China

  1. †

    Xueqing Xing and Quan Liu contributed equally to this work.

*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

  1. †

    Xueqing Xing and Quan Liu contributed equally to this work.

Publication History

  1. Issue published online: 15 DEC 2012
  2. Article first published online: 15 SEP 2012
  3. Accepted manuscript online: 14 AUG 2012 01:00AM EST
  4. Manuscript Accepted: 28 JUL 2012
  5. Manuscript Revised: 19 JUL 2012
  6. Manuscript Received: 30 JAN 2012

Funded by

  • National Natural Scientific Foundation of China. Grant Number: 10385008
  • The Knowledge Innovation Program of Chinese Academy of Sciences. Grant Number: kjcx3.syw.n8
  • The Momentous Equipment Program of Chinese Academy of Sciences. Grant Numbers: YZ200829, 973 projects, 2003CB114204, 863 projects, 2006AA10A210
  • The Ministry of Science and Beijing grand project. Grant Number: D706005040431
  • National Natural Scientific Foundation of China. Grant Number: 31101485

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Keywords:

  • domain;
  • structure restoration;
  • structure prediction;
  • SRCD;
  • SAXS;
  • PeaT1

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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