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VAT-1 from Torpedo synaptic vesicles is a calcium binding protein: a study in bacterial expression systems.

Abstract：

:1. Calcium binding properties were examined in VAT-1, an abundant 41-kDa membrane protein expressed in the cholinergic cynaptic vesicles of Torpedo. 2. An overlay assay, using 45Ca2+ as a tracer, demonstrated the ability of a recombinant VAT-1 produced from the IPTG-inducible pKK223-3 expression vector to bind calcium. 3. A high yield of recombinant VAT-1 was obtained from the glutathione S-transferase (GST) expression system. The fusion product enabled VAT-1 purification via affinity chromatography. Subsequent cleavage by thrombin resulted in its separation from the GST carrier protein. 4. A direct Ca(2+)-binding study was performed with purified VAT-1 by a quick-spin column technique, in the presence of 45Ca2+. Quantitative analysis revealed a 1:1 molar stoichiometry for binding of Ca2+ to VAT-1, with a dissociation constant of 130 microM. 5. A GST-linked truncated protein consisting of 13 kDa from the VAT-1 carboxy-terminal domain was found to retain the capacity to bind Ca2+. 6. A data search for homologies between VAT-1 and known Ca(2+)-binding proteins revealed considerable similarity to members of the annexin family in a 140-amino acid region from the carboxy terminal of VAT-1, which overlaps two tandem Ca(2+)-binding domains of the annexin proteins.

journal_name

Cell Mol Neurobiol

journal_title

Cellular and molecular neurobiology

authors

Levius O,Linial M

doi

10.1007/BF00711457

subject

Has Abstract

pub_date

1993-10-01 00:00:00

pages

483-92

issue

5

eissn

0272-4340

issn

1573-6830

journal_volume

13

pub_type

杂志文章

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