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The Caenorhabditis elegans Avermectin Resistance and Anesthetic Response Gene unc‐9 Encodes a Member of a Protein Family Implicated in Electrical Coupling of Excitable Cells
Author(s) -
Barnes T. M.,
Hekimi S.
Publication year - 1997
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.1997.69062251.x
Subject(s) - caenorhabditis elegans , mutant , biology , gene , phenotype , genetics , positional cloning , microbiology and biotechnology , mutation , avermectin , anatomy
Mutations in the unc‐9 gene of the nematode Caenorhabditis elegans cause abnormal forward locomotion and an egg‐retention phenotype. unc‐9 mutations also reduce the worms' sensitivity to avermectin and block a form of hypersensitivity to volatile anesthetics. We report here the cloning and molecular characterization of unc‐9 and show that it encodes a member of the OPUS family of proteins that is 56% identical to another OPUS protein, UNC‐7. It is significant that unc‐9 mutants share all phenotypes with unc‐7 mutants. Mutants in another gene, unc‐124 , also share all tested phenotypes with unc‐9 mutants, including identical locomotory and egg‐laying defects, suggesting that multiple genes are required for the same biochemical function. OPUS proteins are implicated in the function of invertebrate gap junctions, and, based on a new alignment including 24 members from C. elegans , we present a refined model for the structure of OPUS proteins suggesting that oligomers could form a hydrophilic pore. We also show that alteration of highly conserved proline residues in UNC‐9 leads to a cold sensitivity that likely affects a step in protein expression rather than function. Finally, we speculate on the basis of the avermectin resistance and anesthetic response phenotypes.

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