Coevolution study of mitochondria respiratory chain proteins: Toward the understanding of protein–protein interaction

Ming Yang; Yan Ge; Jiayan Wu; Jingfa Xiao; Jun Yu

doi:10.1016/j.jgg.2011.04.003

Volume 38 Issue 5

May 2011

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Article Navigation > Journal of Genetics and Genomics > 2011 > 38(5): 201-207

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Coevolution study of mitochondria respiratory chain proteins: Toward the understanding of protein–protein interaction

doi: 10.1016/j.jgg.2011.04.003

a
CAS Key Laboratory of Genome Sciences and Information, Beijing Institute of Genomics, Chinese Academy of Sciences, Beijing 100029, China
b
Graduate University of Chinese Academy of Sciences, Beijing 100049, China
c
College of Biology, China Agricultural University, Beijing 100091, China

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Corresponding author: E-mail address: xiaojingfa@big.ac.cn (Jingfa Xiao); E-mail address: junyu@big.ac.cn (Jun Yu)
Received Date: 2011-01-20
Accepted Date: 2011-04-09
Rev Recd Date: 2011-04-08

Available Online: 2011-04-15

Publish Date: 2011-05-20

Abstract

Abstract

Coevolution can be seen as the interdependency between evolutionary histories. In the context of protein evolution, functional correlation proteins are ever-present coordinated evolutionary characters without disruption of organismal integrity. As to complex system, there are two forms of protein–protein interactions in vivo, which refer to inter-complex interaction and intra-complex interaction. In this paper, we studied the difference of coevolution characters between inter-complex interaction and intra-complex interaction using “Mirror tree” method on the respiratory chain (RC) proteins. We divided the correlation coefficients of every pairwise RC proteins into two groups corresponding to the binary protein–protein interaction in intra-complex and the binary protein–protein interaction in inter-complex, respectively. A dramatical discrepancy is detected between the coevolution characters of the two sets of protein interactions (Wilcoxon test, p-value = 4.4 × 10⁻⁶). Our finding reveals some critical information on coevolutionary study and assists the mechanical investigation of protein–protein interaction. Furthermore, the results also provide some unique clue for supramolecular organization of protein complexes in the mitochondrial inner membrane. More detailed binding sites map and genome information of nuclear encoded RC proteins will be extraordinary valuable for the further mitochondria dynamics study.
- Coevolution,
- Respiratory chain proteins,
- “Mirror tree” method,
- Supercomplex,
- Protein–protein interaction

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References(32)

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