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Genomic structure of the amphioxus calcium vector protein
1Biological Institute, Graduate School of Science, Tohoku University, Sendai, 980-8578, Japan.
Journal of Biochemistry
|September 1, 1999
Summary
Calcium vector protein (CaVP) in amphioxus likely belongs to the troponin C superfamily. Gene structure analysis reveals conserved intron positions, suggesting evolutionary links to other Ca(2+)-binding proteins.
Area of Science:
- Evolutionary biology
- Molecular biology
- Biochemistry
Background:
- Calcium vector protein (CaVP) is a unique EF-hand Ca(2+)-binding protein found in amphioxus.
- Its precise function as a Ca(2+) signal transducer and its evolutionary relationships are not well understood.
Purpose of the Study:
- To investigate the evolutionary origins and relationships of CaVP.
- To elucidate the gene structure of CaVP and compare it with related Ca(2+)-binding proteins.
Main Methods:
- Sequencing of CaVP cDNAs from two amphioxus species (Branchiostoma lanceolatum and B. floridae).
- Gene structure elucidation of B. floridae CaVP, including exon-intron organization.
- Comparative analysis of intron positions with calmodulin, troponin C, and Spec proteins.
Main Results:
- High sequence identity (96.5% cDNA, 98.2% amino acid) between CaVP from the two studied amphioxus species.
- The CaVP gene comprises seven exons and six introns.
- Four intron positions are conserved with calmodulin, troponin C, and Spec proteins, indicating CaVP belongs to the troponin C superfamily.
- One intron is unique to CaVP, potentially marking its lineage.
- The position of another intron is not conserved, suggesting evolutionary events like intron sliding or addition.
Conclusions:
- CaVP is likely a member of the troponin C superfamily, based on conserved intron positions.
- The unique intron in CaVP may serve as a lineage-specific marker.
- Gene structure analysis provides insights into the evolution of Ca(2+)-binding proteins.