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Originally published In Press as doi:10.1074/jbc.M006308200 on October 2, 2000

J. Biol. Chem., Vol. 276, Issue 1, 464-474, January 5, 2001
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Zebrafish Acetylcholinesterase Is Encoded by a Single Gene Localized on Linkage Group 7
GENE STRUCTURE AND POLYMORPHISM; MOLECULAR FORMS AND EXPRESSION PATTERN DURING DEVELOPMENT*

Christelle BertrandDagger , Arnaud ChatonnetDagger , Christina TakkeDagger , YiLin Yan§, John Postlethwait§, Jean-Pierre ToutantDagger , and Xavier CousinDagger

From the Dagger  Différenciation Cellulaire et Croissance, INRA, 2 Place Viala, 34060 Montpellier Cedex, France and the § Institute of Neuroscience, University of Oregon, Eugene, Oregon 97403

We cloned and sequenced the acetylcholinesterase gene and cDNA of zebrafish, Danio rerio. We found a single gene (ache) located on linkage group LG7. The relative organization of ache, eng2, and shh genes is conserved between zebrafish and mammals and defines a synteny. Restriction fragment length polymorphism analysis was allowed to identify several allelic variations. We also identified two transposable elements in non-coding regions of the gene. Compared with other vertebrate acetylcholinesterase genes, ache gene contains no alternative splicing at 5' or 3' ends where only a T exon is present. The translated sequence is 60-80% identical to acetylcholinesterases of the vertebrates and exhibits an extra loop specific to teleosts. Analysis of molecular forms showed a transition, at the time of hatching, from the globular G4 form to asymmetric A12 form that becomes prominent in adults. In situ hybridization and enzymatic activity detection on whole embryos confirmed early expression of the acetylcholinesterase gene in nervous and muscular tissues. We found no butyrylcholinesterase gene or activity in Danio. These findings make zebrafish a promising model to study function of acetylcholinesterase during development and regulation of molecular forms assembly in vivo.


* This research work was supported by grants from Association Française contre les Myopathies (to X. C., J.-P. T., and A. C.) and National Institutes of Health Grant P01HD22486 (to J.-H. P. and Y. Y.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AJ251640 (for ache) and AF003943 (for esterase).

To whom correspondence should be addressed: Différenciation Cellulaire et Croissance, INRA, 2 Place Viala, 34060 Montpellier Cedex, France. Tel.: 33 4 99 61 28 14; Fax: 33 4 67 54 56 94; E-mail: cousin@ensam.inra.fr.


Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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Toxicol SciHome page
M. Behra, C. Etard, X. Cousin, and U. Strahle
The Use of Zebrafish Mutants to Identify Secondary Target Effects of Acetylcholine Esterase Inhibitors
Toxicol. Sci., February 1, 2004; 77(2): 325 - 333.
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