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Proposed function of alternative oxidase in mitochondrial sulphide oxidation detoxification in the Echiuran worm, Urechis unicinctus

Published online by Cambridge University Press:  22 July 2013

Jian Huang ,
Litao Zhang ,
Jinlong Li ,
Xiaoli Shi  and
Zhifeng Zhang
Jian Huang
Affiliation:
Key Laboratory of Marine Genetics and Breeding (Ocean University of China), Ministry of Education, Qingdao 266003, China
Litao Zhang
Affiliation:
Key Laboratory of Marine Genetics and Breeding (Ocean University of China), Ministry of Education, Qingdao 266003, China
Jinlong Li
Affiliation:
Key Laboratory of Marine Genetics and Breeding (Ocean University of China), Ministry of Education, Qingdao 266003, China
Xiaoli Shi
Affiliation:
Key Laboratory of Marine Genetics and Breeding (Ocean University of China), Ministry of Education, Qingdao 266003, China
Zhifeng Zhang*
Affiliation:
Key Laboratory of Marine Genetics and Breeding (Ocean University of China), Ministry of Education, Qingdao 266003, China
*
Correspondence should be addressed to: Z. Zhang, Key Laboratory of Marine Genetics and Breeding (Ocean University of China), Ministry of Education, Qingdao 266003, China email: [email protected].
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Abstract

Alternative oxidase (AOX), a ubiquinol oxidase, introduces a branch pathway to the respiratory electron transport chain (ETC), bypassing complexes III and IV and catalysing the cyanide-resistant reduction of oxygen to water without translocation of protons across the inner mitochondrial membrane. Thus, it functions as a non-energy-conserving member of respiratory ETC. Previous studies of AOX focused on plants and some fungi, whereas data on animals are limited. In this study, full-length AOX cDNA was cloned from the Echiuran worm, Urechis unicinctus, a marine benthic invertebrate. In addition, mRNA expression pattern of combined activity of cytochrome c oxidase (CCO) in the body wall and hindgut of the worm exposed in sulphide (50 µM and 150 µM) was measured. The results revealed that AOX mRNA expression increased in a time- and concentration-dependent manner in both tissues, was significantly increased at 48 h, and continuously increased with time. In contrast, the activity of CCO decreased significantly at 24 h and was inhibited at 48 h during exposure to 150 µM sulphide. The present data indicate the expression of AOX mRNA depended on the sulphide concentration present as well as being influenced by the physical condition of the worm, especially the CCO activity.

Keywords

alternative oxidasecytochrome c oxidasesulphideUrechis unicinctus
Type
Research Article
Information
Journal of the Marine Biological Association of the United Kingdom , Volume 93 , Issue 8 , December 2013 , pp. 2145 - 2154
Copyright
Copyright © Marine Biological Association of the United Kingdom 2013 

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Footnotes

*

Joint first authors

References

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