Identification of a calmodulin-regulated autoinhibited Ca2+-ATPase (ACA11) that is localized to vacuole membranes in Arabidopsisopen access
- Authors
- Lee, Sang Min; Kim, Ho Soo; Han, Hay Ju; Moon, Byeong Cheol; Kim, Cha Young; Harper, Jeffery F.; Chung, Woo Sik
- Issue Date
- 21-Aug-2007
- Publisher
- WILEY
- Keywords
- Ca2+-ATPase; calcium; calmodulin; membrane; protein; vacuole; Arabidopsis
- Citation
- FEBS LETTERS, v.581, no.21, pp 3943 - 3949
- Pages
- 7
- Indexed
- SCIE
SCOPUS
- Journal Title
- FEBS LETTERS
- Volume
- 581
- Number
- 21
- Start Page
- 3943
- End Page
- 3949
- URI
- https://scholarworks.gnu.ac.kr/handle/sw.gnu/28303
- DOI
- 10.1016/j.febslet.2007.07.023
- ISSN
- 0014-5793
1873-3468
- Abstract
- In plant cells, the vacuole functions as a major calcium store. Although a calmodulin-regulated Ca2+-ATPase (ACA4) is known to be present 2 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. Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
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