VAT‐1 from Torpedo is a membranous homologue of zeta crystallin
- 2 January 1993
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 315 (1), 91-94
- https://doi.org/10.1016/0014-5793(93)81140-u
Abstract
VAT-1 is a major protein from Torpedo synaptic vesicles. A protein data-base search revealed a striking homology to zeta 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 zeta 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.Keywords
This publication has 17 references indexed in Scilit:
- Lens protein expression in mammals: Taxon-specificity and the recruitment of crystallinsJournal of Molecular Evolution, 1991
- Eukaryotic proteins expressed in Escherichia coli: An improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferaseAnalytical Biochemistry, 1991
- Zeta-crystallin, a novel protein from the guinea pig lens is related to alcohol dehydrogenasesGene, 1989
- Enzyme/crystallins: Gene sharing as an evolutionary strategyCell, 1989
- VAT 1: An abundant membrane protein from torpedo cholinergic synaptic vesiclesNeuron, 1989
- LENS CRYSTALLINS: THE EVOLUTION AND EXPRESSION OF PROTEINS FOR A HIGHLY SPECIALIZED TISSUEAnnual Review of Biochemistry, 1988
- Zeta-crystallin, a novel lens protein from the guinea pigCurrent Eye Research, 1987
- A comprehensive set of sequence analysis programs for the VAXNucleic Acids Research, 1984
- DNA sequencing with chain-terminating inhibitorsProceedings of the National Academy of Sciences of the United States of America, 1977
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970