VAT-1 from Torpedo is a membranous homologue of zeta crystallin

Michael Linial; Orit Levius

doi:10.1016/0014-5793(93)81140-U

VAT-1 from Torpedo is a membranous homologue of zeta crystallin

Michael Linial^*, Orit Levius

^*Corresponding author for this work

Department of Biological Chemistry

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

24 Scopus citations

Abstract

VAT-1 is a major protein from Torpedo synaptic vesicles. A protein data-base search revealed a striking homology to ξ crystallin from guinea pig lens. The overall amino-acid identity is 27%, and 58% similarity is reached by including conserved substitutions. The highest similarity (60% to 85%) between the two proteins is observed in five discrete domains, which are also conserved in zinc-dependent dehydrogenases, particularly in the alcohol dehydrogenase family. The cofactor-binding domain of oxidoreductases is conserved in VAT-1 and in ξ crystallin. VAT-1 preferably binds NADPH in the presence of zinc. In contrast with its homologous proteins, VAT-1 is an integral membrane protein of synaptic vesicles.

Original language	English
Pages (from-to)	91-94
Number of pages	4
Journal	FEBS Letters
Volume	315
Issue number	1
DOIs	https://doi.org/10.1016/0014-5793(93)81140-U
State	Published - 2 Jan 1993

Bibliographical note

Funding Information:
Acknowjledgements: We wish to thank Dr. D.M. Michaelson, Dept. of Neurochemistry, Tel Aviv University, for providing Torpedo tissue and to D. Parnas for critically reading of the manuscript. This work was partially supported by the US-Israel Binational Foundation (Grant 89-00209).

Keywords

Electric organ
Lens crystallin
Oxidoreductase
Protein evolution
Synaptic vesicle

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title = "VAT-1 from Torpedo is a membranous homologue of zeta crystallin",

abstract = "VAT-1 is a major protein from Torpedo synaptic vesicles. A protein data-base search revealed a striking homology to ξ crystallin from guinea pig lens. The overall amino-acid identity is 27%, and 58% similarity is reached by including conserved substitutions. The highest similarity (60% to 85%) between the two proteins is observed in five discrete domains, which are also conserved in zinc-dependent dehydrogenases, particularly in the alcohol dehydrogenase family. The cofactor-binding domain of oxidoreductases is conserved in VAT-1 and in ξ crystallin. VAT-1 preferably binds NADPH in the presence of zinc. In contrast with its homologous proteins, VAT-1 is an integral membrane protein of synaptic vesicles.",

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note = "Funding Information: Acknowjledgements: We wish to thank Dr. D.M. Michaelson, Dept. of Neurochemistry, Tel Aviv University, for providing Torpedo tissue and to D. Parnas for critically reading of the manuscript. This work was partially supported by the US-Israel Binational Foundation (Grant 89-00209).",

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AU - Levius, Orit

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AB - VAT-1 is a major protein from Torpedo synaptic vesicles. A protein data-base search revealed a striking homology to ξ crystallin from guinea pig lens. The overall amino-acid identity is 27%, and 58% similarity is reached by including conserved substitutions. The highest similarity (60% to 85%) between the two proteins is observed in five discrete domains, which are also conserved in zinc-dependent dehydrogenases, particularly in the alcohol dehydrogenase family. The cofactor-binding domain of oxidoreductases is conserved in VAT-1 and in ξ crystallin. VAT-1 preferably binds NADPH in the presence of zinc. In contrast with its homologous proteins, VAT-1 is an integral membrane protein of synaptic vesicles.

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KW - Lens crystallin

KW - Oxidoreductase

KW - Protein evolution

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VAT-1 from Torpedo is a membranous homologue of zeta crystallin

Abstract

Bibliographical note

Keywords

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