Journal of Tropical Oceanography ›› 2021, Vol. 40 ›› Issue (2): 27-38.doi: 10.11978/2020055CSTR: 32234.14.2020055

• Marine Biology • Previous Articles     Next Articles

Functional study of coupling protein CheV and CZB domain of chemoreceptors in the Epsilon-proteobacteria chemotaxis signaling pathway

LIU Yugeng1,2(), MAO Yingjin1,2, ZHANG Canchuan1,2, GAO Beile1()   

  1. 1. CAS Key Laboratory of Tropical Marine Bio-resources and Ecology, Guangdong Key Laboratory of Marine Materia Medica, South China Sea Institute of Oceanology, Chinese Academy of Sciences, Guangzhou 510301, China
    2. University of Chinese Academy of Sciences, Beijing 100049, China
  • Received:2020-05-26 Revised:2020-06-29 Online:2021-03-10 Published:2020-07-29
  • Contact: GAO Beile E-mail:yugengliu@163.com;gaob@scsio.ac.cn
  • Supported by:
    National Science Foundation of China(31870064)

Abstract:

Epsilon-proteobacteria is widely distributed, from deep-sea hydrothermal vent to surface sea water, from free-living environment to host-associated one. Chemotaxis plays an important role in bacteria survival through sensing and responding to environmental changes. Thus, some bacteria have evolved into many complex and diverse chemotaxis systems. Epsilon-proteobacteria can adapt to different environments; especially, some species can survive in the deep-sea extreme environments including hydrothermal vent and cold seep, whose chemotaxis system may have special characteristics. Bioinformatics analyses by BlastP and MIST database revealed that most Epsilon-proteobacteria species in the deep-sea hydrothermal vent have F3 type chemotaxis system. They all contain a single copy of CheV, which is a double domain fusion protein. Besides, a unique domain, CZB (C-terminal Zinc-Binding) domain, exists in chemoreceptors of deep-sea Epsilon- proteobacteria. A CZB-like domain is also identified in Epsilon-proteobacteria. Using the model strain Campylobacter jejuni 81-176, we confirmed that CheV can interact with all chemoreceptors with MA domain by bacterial two-hybrid experiments. Additionally, we demonstrated that CZB-like domain cannot bind Zn by ICP-Mass, but it can promote the interaction between chemoreceptor Tlp9 and CheV.

Key words: Epsilon-proteobacteria, chemotaxis, CheV, CZB domain

CLC Number: 

  • P735.4