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Regulatory role of the N terminus of the vacuolar calcium-ATPase in cauliflower
Department of Plant Biochemistry, Lund University, Lund, Sweden.
Department of Plant Biochemistry, Lund University, Lund, Sweden.
Jönköping University, School of Education and Communication, HLK, Disciplinary Research. Department of Plant Biochemistry, Lund University, Lund, Sweden.ORCID iD: 0000-0003-0117-2974
2000 (English)In: Plant Physiology, ISSN 0032-0889, E-ISSN 1532-2548, Vol. 122, no 2, 517-526 p.Article in journal (Refereed) Published
Abstract [en]

The vacuolar calmodulin (CaM)-stimulated Ca2+-ATPase, BCA1p, in cauliflower (Brassica oleracea) has an extended N terminus, which was suggested to contain a CaM-binding domain (S. Malmstrom, P. Askerlund, M.G. Palmgren [1997] FEBS Lett 400: 324328). The goal of the present study was to determine the role of the N terminus in regulating BCA1p. Western analysis using three different antisera showed that the N terminus of BCA1p is cleaved off by trypsin and that the N terminus contains the CaM-binding domain. Furthermore, the expressed N terminus binds CaM in a Ca2+dependent manner. A synthetic peptide corresponding to the CaM-binding domain of BCA1p (Ala-19 to Leu-43) strongly inhibited ATP-dependent Ca2+ pumping by BCA1p in cauliflower low-density membranes, indicating that the CaM-binding region of BCA1p also has an autoinhibitory function. The expressed N terminus of BCA1p and a synthetic peptide (Ala-19 to Met-39) were good substrates for phosphorylation by protein kinase C. Sequencing of the phosphorylated fusion protein and peptide suggested serine-16 and/or serine-28 as likely targets for phosphorylation. Phosphorylation of serine-28 had no effect on CaM binding to the alanine-19 to methionine-39 peptide. Our results demonstrate the regulatory importance of the N terminus of BCA1p as a target for CaM binding, trypsin cleavage, and phosphorylation, as well as its importance as an autoinhibitory domain.

Place, publisher, year, edition, pages
2000. Vol. 122, no 2, 517-526 p.
Keyword [en]
Amino Acid Sequence, Base Sequence, Brassica/*enzymology, Calcium/metabolism, Calcium-Transporting ATPases/chemistry/*metabolism, Calmodulin/metabolism, DNA Primers, Ion Transport, Molecular Sequence Data, Phosphorylation, Plant Roots, Protein Binding, Protein Kinase C/metabolism, RNA; Messenger/genetics/metabolism, Vacuoles/*enzymology
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:hj:diva-2171PubMedID: 10677444OAI: oai:DiVA.org:hj-2171DiVA: diva2:32991
Available from: 2007-10-17 Created: 2007-10-17 Last updated: 2017-02-13Bibliographically approved

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