Piezophilic Phenotype Is Growth Condition Dependent and Correlated with the Regulation of Two Sets of ATPase in Deep-Sea Piezophilic Bacterium Photobacterium profundum SS9

Author:

Li An-Qi123,Zhang Wei-Jia345ORCID,Li Xue-Gong345,Bao Xu-Chong23,Qi Xiao-Qing345,Wu Long-Fei46ORCID,Bartlett Douglas H.7

Affiliation:

1. Institute of Oceanology, Chinese Academy of Sciences, Qingdao 266071, China

2. University of Chinese Academy of Sciences, Beijing 101408, China

3. Laboratory of Deep-Sea Microbial Cell Biology, Institute of Deep-sea Science and Engineering, Chinese Academy of Sciences, Sanya 572000, China

4. International Associated Laboratory of Evolution and Development of Magnetotactic Multicellular Organisms, CNRS-Marseille/CAS-Sanya, Sanya 572000, China

5. Institution of Deep-sea Life Sciences, IDSSE-BGI, Hainan Deep-sea Technology Laboratory, Sanya 572000, China

6. LCB, Aix Marseille University and CNRS, 13402 Marseille, France

7. Marine Biology Research Division, Scripps Institution of Oceanography, University of California San Diego, La Jolla, CA 92093, USA

Abstract

Alteration of respiratory components as a function of pressure is a common strategy developed in deep-sea microorganisms, presumably to adapt to high hydrostatic pressure (HHP). While the electron transport chain and terminal reductases have been extensively studied in deep-sea bacteria, little is known about their adaptations for ATP generation. In this study, we showed that the deep-sea bacterium Photobacterium profundum SS9 exhibits a more pronounced piezophilic phenotype when grown in minimal medium supplemented with glucose (MG) than in the routinely used MB2216 complex medium. The intracellular ATP level varied with pressure, but with opposite trends in the two culture media. Between the two ATPase systems encoded in SS9, ATPase-I played a dominant role when cultivated in MB2216, whereas ATPase-II was more abundant in the MG medium, especially at elevated pressure when cells had the lowest ATP level among all conditions tested. Further analyses of the ΔatpI, ΔatpE1 and ΔatpE2 mutants showed that disrupting ATPase-I induced expression of ATPase-II and that the two systems are functionally redundant in MB2216. Collectively, we provide the first examination of the differences and relationships between two ATPase systems in a piezophilic bacterium, and expanded our understanding of the involvement of energy metabolism in pressure adaptation.

Funder

Key Research and Development Program of Hainan Province

National Natural Science Foundation of China

Sanya city

Publisher

MDPI AG

Subject

Virology,Microbiology (medical),Microbiology

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