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Structure, function and regulation of plasma membrane H(+)-ATPase
1Departamento de Biotecnologia, Universidad Politécnica, Valencia, Spain.
FEBS Letters
|June 28, 1993
Summary
Key antigenic sites of yeast ATPase are in the N-terminus, while the C-terminus acts as an auto-inhibitory domain. Functional plant ATPases expressed in yeast enable mutational analysis for understanding active transport mechanisms.
Area of Science:
- Molecular Biology
- Plant Physiology
- Biochemistry
Background:
- The N-terminal region of yeast ATPase contains most antigenic determinants.
- Specific amino acids (24-56) are crucial for plasma membrane insertion and are highly accessible.
- The C-terminus functions as a modulable auto-inhibitory domain in both yeast and plant ATPases.
Purpose of the Study:
- To analyze plant ATPases using functional expression in yeast.
- To investigate the role of ATPase in plant active transport.
- To provide molecular evidence for the 'Acid growth' theory.
Main Methods:
- Expression of functional plant enzyme in yeast for mutational analysis.
- Localization studies in plant tissues involved in active transport.
- Analysis of auxin's effect on ATPase synthesis in corn coleoptiles.
Main Results:
- Plant ATPases can be functionally expressed and mutated in yeast.
- ATPase is abundant in plant tissues facilitating active transport (stomata, phloem, root epidermis, endodermis).
- A specific ATPase isoform is phloem-specific.
- Auxin induces ATPase synthesis in corn coleoptiles, supporting the 'Acid growth' theory.
Conclusions:
- The N-terminus of yeast ATPase harbors critical antigenic sites, and the C-terminus acts as a regulatory domain.
- Functional expression in yeast is a viable method for plant ATPase mutational analysis.
- ATPase plays a significant role in plant active transport, with specific isoforms and auxin regulation contributing to physiological processes like 'Acid growth'.