The protein VAT-1 from Torpedo electric organ exhibits an ATPase activity

Michal Linial; Orit Levius

doi:10.1016/0304-3940(93)90506-G

The protein VAT-1 from Torpedo electric organ exhibits an ATPase activity

Michal Linial^*, Orit Levius

^*Corresponding author for this work

Department of Biological Chemistry

Research output: Contribution to journal › Article › peer-review

16 Scopus citations

Abstract

VAT-1 is an abundant protein in Torpedo electric organ which copurifies with a major ATPase activity from synaptic vesicles. VAT-1 was expressed in E. coli and the product was purified and analyzed. The protein binds specifically to an ATP column and displays an ATPase activity as measured by the kinetics of [³²P]phosphate release. The activity is dependent on divalent ions, with both Mg²⁺ and Ca²⁺ supporting the reaction. The apparent K_m for ATP is 18 μM. This ATPase activity is not affected by known inhibitors of the vesicular V- and P-type ATPases such as vanadate and N-ethylmaleimide. We suggest that VAT-1 activity may affect ATP-dependent reactions in Torpedo nerve terminals, such as phosphorylation and dephosphorylation of proteins.

Original language	English
Pages (from-to)	155-157
Number of pages	3
Journal	Neuroscience Letters
Volume	152
Issue number	1-2
DOIs	https://doi.org/10.1016/0304-3940(93)90506-G
State	Published - 2 Apr 1993

Bibliographical note

Funding Information:
This work was supported in part by US-Israel BSF Grant 209-89 and by the National Institute for Psychobiology in Israel. M.L. is a member of the Otto Lewie Center for Molecular and Cellular Neurobiology in Jerusalem.

Keywords

Adenosine triphosphatase
Electric organ
Expression vector
Nerve terminal
Synaptic vesicle protein
Torpedo

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10.1016/0304-3940(93)90506-G

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title = "The protein VAT-1 from Torpedo electric organ exhibits an ATPase activity",

abstract = "VAT-1 is an abundant protein in Torpedo electric organ which copurifies with a major ATPase activity from synaptic vesicles. VAT-1 was expressed in E. coli and the product was purified and analyzed. The protein binds specifically to an ATP column and displays an ATPase activity as measured by the kinetics of [32P]phosphate release. The activity is dependent on divalent ions, with both Mg2+ and Ca2+ supporting the reaction. The apparent Km for ATP is 18 μM. This ATPase activity is not affected by known inhibitors of the vesicular V- and P-type ATPases such as vanadate and N-ethylmaleimide. We suggest that VAT-1 activity may affect ATP-dependent reactions in Torpedo nerve terminals, such as phosphorylation and dephosphorylation of proteins.",

keywords = "Adenosine triphosphatase, Electric organ, Expression vector, Nerve terminal, Synaptic vesicle protein, Torpedo",

author = "Michal Linial and Orit Levius",

note = "Funding Information: This work was supported in part by US-Israel BSF Grant 209-89 and by the National Institute for Psychobiology in Israel. M.L. is a member of the Otto Lewie Center for Molecular and Cellular Neurobiology in Jerusalem.",

year = "1993",

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doi = "10.1016/0304-3940(93)90506-G",

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AU - Linial, Michal

AU - Levius, Orit

N1 - Funding Information: This work was supported in part by US-Israel BSF Grant 209-89 and by the National Institute for Psychobiology in Israel. M.L. is a member of the Otto Lewie Center for Molecular and Cellular Neurobiology in Jerusalem.

PY - 1993/4/2

Y1 - 1993/4/2

N2 - VAT-1 is an abundant protein in Torpedo electric organ which copurifies with a major ATPase activity from synaptic vesicles. VAT-1 was expressed in E. coli and the product was purified and analyzed. The protein binds specifically to an ATP column and displays an ATPase activity as measured by the kinetics of [32P]phosphate release. The activity is dependent on divalent ions, with both Mg2+ and Ca2+ supporting the reaction. The apparent Km for ATP is 18 μM. This ATPase activity is not affected by known inhibitors of the vesicular V- and P-type ATPases such as vanadate and N-ethylmaleimide. We suggest that VAT-1 activity may affect ATP-dependent reactions in Torpedo nerve terminals, such as phosphorylation and dephosphorylation of proteins.

AB - VAT-1 is an abundant protein in Torpedo electric organ which copurifies with a major ATPase activity from synaptic vesicles. VAT-1 was expressed in E. coli and the product was purified and analyzed. The protein binds specifically to an ATP column and displays an ATPase activity as measured by the kinetics of [32P]phosphate release. The activity is dependent on divalent ions, with both Mg2+ and Ca2+ supporting the reaction. The apparent Km for ATP is 18 μM. This ATPase activity is not affected by known inhibitors of the vesicular V- and P-type ATPases such as vanadate and N-ethylmaleimide. We suggest that VAT-1 activity may affect ATP-dependent reactions in Torpedo nerve terminals, such as phosphorylation and dephosphorylation of proteins.

KW - Adenosine triphosphatase

KW - Electric organ

KW - Expression vector

KW - Nerve terminal

KW - Synaptic vesicle protein

KW - Torpedo

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JO - Neuroscience Letters

JF - Neuroscience Letters

IS - 1-2

ER -

The protein VAT-1 from Torpedo electric organ exhibits an ATPase activity

Abstract

Bibliographical note

Keywords

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