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Auto-inhibition of Arabidopsis thaliana plasma membrane Ca2+-ATPase involves an interaction of the N-terminus with the small cytoplasmic loop
- Source :
-
FEBS Letters . Sep2004, Vol. 574 Issue 1-3, p20-24. 5p. - Publication Year :
- 2004
-
Abstract
- Type IIB Ca2+-ATPases have a terminal auto-inhibitory, domain the action of which is suppressed by calmodulin (CaM) binding. Here, we show that a peptide (6His-1M-I116) corresponding to the first 116 aminoacids (aa) of At-ACA8, the first cloned isoform of Arabidopsis thaliana plasma membrane Ca2+-ATPase, inhibits the activity of the enzyme deprived of the N-terminus by controlled trypsin treatment 10-fold more efficiently than a peptide (41I-T63) corresponding only to the CaM-binding site. A peptide (268E-W348) corresponding to 81 aa of the small cytoplasmic loop of At-ACA8 binds peptide 6His-1M-I116 immobilized on Ni–NTA agarose. Peptide 268E-W348 stimulates Ca2+-ATPase activity. Its effect is not additive with that of CaM and is suppressed by tryptic cleavage of the N-terminus. These results provide the first functional identification of a site of intramolecular interaction with the terminal auto-inhibitory domain of type IIB Ca2+-ATPases. [Copyright &y& Elsevier]
- Subjects :
- *ARABIDOPSIS thaliana
*CELL membranes
*PEPTIDES
*CALMODULIN
Subjects
Details
- Language :
- English
- ISSN :
- 00145793
- Volume :
- 574
- Issue :
- 1-3
- Database :
- Academic Search Index
- Journal :
- FEBS Letters
- Publication Type :
- Academic Journal
- Accession number :
- 14375807
- Full Text :
- https://doi.org/10.1016/j.febslet.2004.08.003