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Stability of Na(+)-K(+)-ATPase alpha-subunit isoforms in evolution.
K Takeyasu1, V Lemas, D M Fambrough
1Department of Physiology, University of Virginia School of Medicine, Charlottesville 22908.
The American Journal of Physiology
|October 1, 1990
Summary
Chicken Na(+)-K(+)-ATPase alpha-subunit isoforms show significant sequence differences within species, suggesting ancient evolutionary divergence. These findings impact understanding of ion transport and enzyme regulation.
Area of Science:
- Biochemistry
- Molecular Biology
- Evolutionary Biology
Background:
- The sodium-potassium pump (Na(+)-K(+)-ATPase) is crucial for cellular function.
- Isoforms of the alpha-subunit contribute to diverse transport activities.
Purpose of the Study:
- To clone and sequence chicken Na(+)-K(+)-ATPase alpha-subunit isoforms (alpha 2 and alpha 3).
- To compare vertebrate alpha-subunit isoform diversity and evolutionary history.
Main Methods:
- DNA cloning and sequencing of chicken Na(+)-K(+)-ATPase alpha-subunit isoforms.
- Bioinformatic analysis and comparison with rat alpha-subunit sequences.
Main Results:
- Nucleotide and amino acid sequences for chicken alpha 2 and alpha 3 isoforms were determined.
- Greater amino acid sequence divergence exists between isoforms within a species than between corresponding bird and mammal isoforms.
- These differences suggest gene duplication and divergence predating avian-mammalian lineage separation.
Conclusions:
- Vertebrate alpha-subunit isoform diversity arose early in evolution.
- Conserved isoform-specific structural features imply functional and regulatory importance for Na(+)-K(+)-ATPase.