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Published on: June 7, 2018
Structure, gene expression, and evolution of primate copper chaperone for superoxide dismutase
Ryoji Fukuhara1, Takashi Kageyama
1Alien Species Research Division, Nansei Environmental Laboratory Co., Ltd., Okinawa, Japan. fukuhara@nansei-kankyo.co.jp
The copper chaperone for superoxide dismutase (CCS) protein is crucial for copper transport in primates, showing high conservation and shared ancestry with Cu,Zn-SOD. Gene expression patterns in monkeys mirror those of Cu,Zn-SOD.
Area of Science:
- Molecular biology
- Evolutionary biology
- Biochemistry
Background:
- Copper chaperone for superoxide dismutase (CCS) facilitates copper delivery to Cu,Zn-superoxide dismutase (Cu,Zn-SOD).
- Understanding CCS evolution and function is vital for cellular redox homeostasis.
Purpose of the Study:
- To investigate the evolutionary conservation and expression patterns of CCS across primate species.
- To elucidate the relationship between CCS and Cu,Zn-SOD evolution.
Main Methods:
- Cloning of CCS cDNAs from six primate species.
- Phylogenetic analysis of CCS and Cu,Zn-SOD proteins.
- Analysis of CCS gene expression in Japanese monkey tissues.
Main Results:
- Primate CCS proteins (274 amino acids) exhibit over 96% similarity, with conserved functional residues.
- Phylogenetic analysis indicates a common ancestor for CCS and Cu,Zn-SOD, diverging early in eukaryote evolution.
- High nonsynonymous substitution rates were observed in the lineage leading to Old World monkeys and apes.
- CCS gene expression is highest in the liver and adrenal gland of Japanese monkeys, similar to Cu,Zn-SOD patterns.
Conclusions:
- Primate CCS is highly conserved, reflecting its essential role in copper transport.
- The evolutionary trajectory of CCS and Cu,Zn-SOD suggests early divergence from a common ancestral gene.
- Tissue-specific expression of CCS in monkeys correlates with Cu,Zn-SOD, implying coordinated regulation.
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