Phylogenetic conservation of disulfide-linked, dimeric acetylcholine receptor pentamers in southern ocean electric rays
Intact acetylcholine receptors have been purified on a novel affinity resin from three electric fish endemic to Australian waters. Their binding properties and morphology are compared with those of their northern hemisphere homolog, Torpedo marmorata . All four exhibit apparent dissociation constant...
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fthighwire:oai:open-archive.highwire.org:jexbio:207/20/3581 2023-05-15T18:25:05+02:00 Phylogenetic conservation of disulfide-linked, dimeric acetylcholine receptor pentamers in southern ocean electric rays Tierney, M. L. Osborn, K. E. Milburn, P. J. Stowell, M. H. B. Howitt, S. M. 2004-09-15 00:00:00.0 text/html http://jeb.biologists.org/cgi/content/short/207/20/3581 https://doi.org/10.1242/jeb.01204 en eng Company of Biologists http://jeb.biologists.org/cgi/content/short/207/20/3581 http://dx.doi.org/10.1242/jeb.01204 Copyright (C) 2004, Company of Biologists Research Article TEXT 2004 fthighwire https://doi.org/10.1242/jeb.01204 2015-02-28T21:59:06Z Intact acetylcholine receptors have been purified on a novel affinity resin from three electric fish endemic to Australian waters. Their binding properties and morphology are compared with those of their northern hemisphere homolog, Torpedo marmorata . All four exhibit apparent dissociation constants, K d , in the nanomolar range for the snake neurotoxin α-bungarotoxin and have a distinctive rosette-like appearance when viewed in negative stain under the electron microscope. Furthermore, these rosettes are paired, indicating that acetylcholine receptors from southern ocean electric fish exist as dimers, in the same fashion as their northern hemisphere counterparts. The cDNAs of the receptor's four subunits were sequenced from Hypnos monopterigium and the northern hemisphere counterpart, Torpedo marmorata , while cDNAs from only two subunits, α and δ, were able to be sequenced from Narcine tasmaniensis. The penultimate amino acid in the δ subunit of each of the newly sequenced fish species is a cysteine residue. Its conservation suggests that the mechanism for the observed dimerization of acetylcholine receptors is disulfide bond formation between the δ subunit of adjacent receptors, analogous to acetylcholine receptor dimers observed in other electric fish. It appears that this mechanism for receptor clustering is unique to acetylcholine receptors packed and organized in the specialized organs of electric fish. Alignment of the deduced protein sequences with the equivalent sequences from Torpedo californica and humans reveals a high degree of homology. Text Southern Ocean HighWire Press (Stanford University) Southern Ocean Journal of Experimental Biology 207 20 3581 3590 |
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HighWire Press (Stanford University) |
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English |
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Research Article |
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Research Article Tierney, M. L. Osborn, K. E. Milburn, P. J. Stowell, M. H. B. Howitt, S. M. Phylogenetic conservation of disulfide-linked, dimeric acetylcholine receptor pentamers in southern ocean electric rays |
topic_facet |
Research Article |
description |
Intact acetylcholine receptors have been purified on a novel affinity resin from three electric fish endemic to Australian waters. Their binding properties and morphology are compared with those of their northern hemisphere homolog, Torpedo marmorata . All four exhibit apparent dissociation constants, K d , in the nanomolar range for the snake neurotoxin α-bungarotoxin and have a distinctive rosette-like appearance when viewed in negative stain under the electron microscope. Furthermore, these rosettes are paired, indicating that acetylcholine receptors from southern ocean electric fish exist as dimers, in the same fashion as their northern hemisphere counterparts. The cDNAs of the receptor's four subunits were sequenced from Hypnos monopterigium and the northern hemisphere counterpart, Torpedo marmorata , while cDNAs from only two subunits, α and δ, were able to be sequenced from Narcine tasmaniensis. The penultimate amino acid in the δ subunit of each of the newly sequenced fish species is a cysteine residue. Its conservation suggests that the mechanism for the observed dimerization of acetylcholine receptors is disulfide bond formation between the δ subunit of adjacent receptors, analogous to acetylcholine receptor dimers observed in other electric fish. It appears that this mechanism for receptor clustering is unique to acetylcholine receptors packed and organized in the specialized organs of electric fish. Alignment of the deduced protein sequences with the equivalent sequences from Torpedo californica and humans reveals a high degree of homology. |
format |
Text |
author |
Tierney, M. L. Osborn, K. E. Milburn, P. J. Stowell, M. H. B. Howitt, S. M. |
author_facet |
Tierney, M. L. Osborn, K. E. Milburn, P. J. Stowell, M. H. B. Howitt, S. M. |
author_sort |
Tierney, M. L. |
title |
Phylogenetic conservation of disulfide-linked, dimeric acetylcholine receptor pentamers in southern ocean electric rays |
title_short |
Phylogenetic conservation of disulfide-linked, dimeric acetylcholine receptor pentamers in southern ocean electric rays |
title_full |
Phylogenetic conservation of disulfide-linked, dimeric acetylcholine receptor pentamers in southern ocean electric rays |
title_fullStr |
Phylogenetic conservation of disulfide-linked, dimeric acetylcholine receptor pentamers in southern ocean electric rays |
title_full_unstemmed |
Phylogenetic conservation of disulfide-linked, dimeric acetylcholine receptor pentamers in southern ocean electric rays |
title_sort |
phylogenetic conservation of disulfide-linked, dimeric acetylcholine receptor pentamers in southern ocean electric rays |
publisher |
Company of Biologists |
publishDate |
2004 |
url |
http://jeb.biologists.org/cgi/content/short/207/20/3581 https://doi.org/10.1242/jeb.01204 |
geographic |
Southern Ocean |
geographic_facet |
Southern Ocean |
genre |
Southern Ocean |
genre_facet |
Southern Ocean |
op_relation |
http://jeb.biologists.org/cgi/content/short/207/20/3581 http://dx.doi.org/10.1242/jeb.01204 |
op_rights |
Copyright (C) 2004, Company of Biologists |
op_doi |
https://doi.org/10.1242/jeb.01204 |
container_title |
Journal of Experimental Biology |
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207 |
container_issue |
20 |
container_start_page |
3581 |
op_container_end_page |
3590 |
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1766206275767500800 |