Identification of a calmodulin-regulated autoinhibited Ca2+-ATPase (ACA11) that is localized to vacuole membranes in Arabidopsis
| Autor: | Byeong Cheol Moon, Cha Young Kim, Jeffery F. Harper, Sang Min Lee, Woo Sik Chung, Hay Ju Han, Ho Soo Kim |
|---|---|
| Jazyk: | angličtina |
| Předmět: |
0106 biological sciences
Calmodulin Calmodulin binding domain ATPase Mutant Biophysics Arabidopsis Vacuole Calcium-Transporting ATPases Saccharomyces cerevisiae Biology 01 natural sciences Biochemistry Plant Roots Green fluorescent protein 03 medical and health sciences Structural Biology Genetics Molecular Biology 030304 developmental biology 0303 health sciences Microscopy Confocal Arabidopsis Proteins Protoplasts Genetic Complementation Test fungi food and beverages Cell Biology biology.organism_classification Plant cell Plants Genetically Modified Cell biology Protein Structure Tertiary Enzyme Activation Membrane protein Vacuoles biology.protein Calcium Ca2+-ATPase 010606 plant biology & botany |
| Zdroj: | FEBS Letters. (21):3943-3949 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/j.febslet.2007.07.023 |
| Popis: | In plant cells, the vacuole functions as a major calcium store. Although a calmodulin-regulated Ca2+-ATPase (ACA4) is known to be present in prevacuolar compartments, the presence of an ACA-type Ca2+-ATPase in the mature vacuole of a plant cell has not been verified. Here we provide evidence that ACA11 localizes to the vacuole membrane. ACA11 tagged with GFP was expressed in stable transgenic plants, and visualized in root cells and protoplasts by confocal microscopy. A Ca2+-ATPase function for ACA11 was confirmed by complementation of yeast mutants. A calmodulin binding domain was identified within the first 37 residues of the N-terminal autoinhibitory region. |
| Databáze: | OpenAIRE |
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