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Structural and functional conservation of synaptotagmin (p65) in Drosophila and humans. by M S Perin; P A Johnston; T Ozcelik; R Jahn; U Francke; T C Südhof is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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Synaptotagmin (p65) is an abundant synaptic vesicle protein that contains two copies of a sequence that is homologous to the regulatory region of protein kinase C. Full length cDNAs encoding human and Drosophila synaptotagmins were characterized to study its structural and functional conservation in evolution. The deduced amino acid sequences for human and rat synaptotagmins show 97% identity, whereas Drosophila and rat synaptotagmins are only 57% identical but exhibit a selective conservation of the two internal repeats that are homologous to the regulatory region of protein kinase C (78% invariant residues in all three species). The two internal repeats of synaptotagmin are only slightly more homologous to each other than to protein kinase C, and the differences between the repeats are conserved in evolution, suggesting that they might not be functionally equivalent. The cytoplasmic domains of human and Drosophila synaptotagmins produced as recombinant proteins in Escherichia coli specifically bound phosphatidylserine similar to rat synaptotagmin. They also hemagglutinated trypsinized erythrocytes at nanomolar concentrations. Hemagglutination was inhibited both by negatively char

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Author

M S Perin; P A Johnston; T Ozcelik; R Jahn; U Francke; T C Südhof

Publisher

Elsevier BV

Published

1991

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)