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ACR-3, a Caenorhabditis elegans nicotinic acetylcholine receptor subunit. Molecular cloning and functional expression
Journal article   Peer reviewed

ACR-3, a Caenorhabditis elegans nicotinic acetylcholine receptor subunit. Molecular cloning and functional expression

H A Baylis, K Matsuda, M D Squire, J T Fleming, Robert J Harvey, M G Darlison, E A Barnard and D B Sattelle
Receptors and Channels, Vol.5(3-4), pp.149-158
1997
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https://www.ncbi.nlm.nih.gov/pubmed/9606719View
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Abstract

acr-3 gene caenorhabditis elegans ligand-gated ion channel nicotinic acetylcholine receptor transient expression xenopus oocytes complementary DNA glycine levamisole mecamylamine membrane protein nicotinic receptor receptor subunit serine
The molecular cloning and functional co-expression of a novel nicotinic acetylcholine receptor (nAChR) non-α subunit gene, acr-3, is described. Previously we determined the sequence and demonstrated the functional co-expression of acr-2, a nAChR non-α subunit gene from Caenorhabditis elegans. Analysis of the acr-2 genomic DNA revealed the existence of another potential nAChR subunit gene, acr-3, in the same orientation, only 281 bp downstream of acr-2. A cDNA containing the entire acr-3 coding sequence was isolated by RT-PCR and sequenced. The predicted protein contains the conserved features typical of nAChR non-α subunits and most closely resembles other invertebrate nAChR non-α polypeptides. Unusually, the highly conserved glycine residue (equivalent to residue 240 in the Torpedo α subunit) upstream of transmembrane domain 2 (m2) is replaced by a serine residue in ACR-3. When acr-3 cDNA was injected alone into Xenopus oocytes no levamisole-gated channel activity was observed. However when co-expressed with a C. elegans α subunit (UNC-38), ACR-3 contributed to the formation of levamisole-gated channels. The response of this hetero-oligomer to levamisole (100 μM) was reduced by the nAChR antagonists mecamylamine (1 μM) and d-tubocurarine (10 μM).

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