Cloning and expression of the vesamicol binding protein from the marine ray Torpedo: Homology with the putative vesicular acetylcholine transporter UNC-17 from Caenorhabditis elegans
Complementary DNA clones corresponding to a messenger RNA encoding a 56 kDa polypeptide have been obtained from Torpedo marmorata and Torpedo ocellata electric lobe libraries, by homology screening with a probe obtained from the putative acetylcholine transporter from the nematode Caenorhabditis ele...
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Veröffentlicht in: | FEBS letters 1994-03, Vol.342 (1), p.97-102 |
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creator | Varoqui, Hélène Diebler, Marie-Françoise Meunier, François-Marie Rand, James B. Usdin, Ted B. Bonner, Tom I. Eiden, Lee E. Erickson, Jeffrey D. |
description | Complementary DNA clones corresponding to a messenger RNA encoding a 56 kDa polypeptide have been obtained from
Torpedo marmorata and
Torpedo ocellata electric lobe libraries, by homology screening with a probe obtained from the putative acetylcholine transporter from the nematode
Caenorhabditis elegans. The
Torpedo proteins display approximately 50% overall identity to the
C. elegans unc-17 protein and 43% identity to the two vesicle monoamine transporters (VMAT1 and VMAT2). This family of proteins is highly conserved within 12 domains which potentially span the vesicle membrane, with little similarity within the putative intraluminal glycosylated loop and at the N- and C-termini. The ~ 3.0 kb mRNA species is specifically expressed in the brain and highly enriched in the electric lobe of
Torpedo. The
Torpedo protein, expressed in CV-1 fibroblast cells, possesses a high-affinity binding site for vesamicol (
K
d = 6 nM), a drug which blocks in vitro and in vivo acetylcholine accumulation in cholinergic vesicles. |
doi_str_mv | 10.1016/0014-5793(94)80592-X |
format | Article |
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Torpedo marmorata and
Torpedo ocellata electric lobe libraries, by homology screening with a probe obtained from the putative acetylcholine transporter from the nematode
Caenorhabditis elegans. The
Torpedo proteins display approximately 50% overall identity to the
C. elegans unc-17 protein and 43% identity to the two vesicle monoamine transporters (VMAT1 and VMAT2). This family of proteins is highly conserved within 12 domains which potentially span the vesicle membrane, with little similarity within the putative intraluminal glycosylated loop and at the N- and C-termini. The ~ 3.0 kb mRNA species is specifically expressed in the brain and highly enriched in the electric lobe of
Torpedo. The
Torpedo protein, expressed in CV-1 fibroblast cells, possesses a high-affinity binding site for vesamicol (
K
d = 6 nM), a drug which blocks in vitro and in vivo acetylcholine accumulation in cholinergic vesicles.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/0014-5793(94)80592-X</identifier><identifier>PMID: 8143858</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Amino Acid Sequence ; Animals ; Base Sequence ; Brain - metabolism ; Caenorhabditis elegans ; Caenorhabditis elegans - chemistry ; Caenorhabditis elegans Proteins ; Caenorhabditis elegans UNC-17 ; Carrier Proteins - chemistry ; Cloning, Molecular ; Glycoproteins - chemistry ; Helminth Proteins - chemistry ; Marine ; Membrane Glycoproteins ; Membrane Transport Proteins ; Molecular Sequence Data ; Neuropeptides ; Piperidines - metabolism ; Receptors, Cholinergic - chemistry ; Receptors, Cholinergic - genetics ; Receptors, Cholinergic - metabolism ; RNA, Messenger - genetics ; RNA, Messenger - metabolism ; Sequence Alignment ; Sequence Homology, Amino Acid ; Torpedo - metabolism ; Torpedo electric lobe ; Torpedo marmorata ; Torpedo ocellata ; Vesamicol ; Vesicular Acetylcholine Transport Proteins ; Vesicular acetylcholine transporter ; Vesicular Biogenic Amine Transport Proteins ; Vesicular Monoamine Transport Proteins ; Vesicular Transport Proteins</subject><ispartof>FEBS letters, 1994-03, Vol.342 (1), p.97-102</ispartof><rights>1994</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c337t-cd1cd50a44d6b300c595b984368b08789c6ca03cf5a2b1322e738759cee6a993</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0014-5793(94)80592-X$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,45974</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8143858$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Varoqui, Hélène</creatorcontrib><creatorcontrib>Diebler, Marie-Françoise</creatorcontrib><creatorcontrib>Meunier, François-Marie</creatorcontrib><creatorcontrib>Rand, James B.</creatorcontrib><creatorcontrib>Usdin, Ted B.</creatorcontrib><creatorcontrib>Bonner, Tom I.</creatorcontrib><creatorcontrib>Eiden, Lee E.</creatorcontrib><creatorcontrib>Erickson, Jeffrey D.</creatorcontrib><title>Cloning and expression of the vesamicol binding protein from the marine ray Torpedo: Homology with the putative vesicular acetylcholine transporter UNC-17 from Caenorhabditis elegans</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Complementary DNA clones corresponding to a messenger RNA encoding a 56 kDa polypeptide have been obtained from
Torpedo marmorata and
Torpedo ocellata electric lobe libraries, by homology screening with a probe obtained from the putative acetylcholine transporter from the nematode
Caenorhabditis elegans. The
Torpedo proteins display approximately 50% overall identity to the
C. elegans unc-17 protein and 43% identity to the two vesicle monoamine transporters (VMAT1 and VMAT2). This family of proteins is highly conserved within 12 domains which potentially span the vesicle membrane, with little similarity within the putative intraluminal glycosylated loop and at the N- and C-termini. The ~ 3.0 kb mRNA species is specifically expressed in the brain and highly enriched in the electric lobe of
Torpedo. The
Torpedo protein, expressed in CV-1 fibroblast cells, possesses a high-affinity binding site for vesamicol (
K
d = 6 nM), a drug which blocks in vitro and in vivo acetylcholine accumulation in cholinergic vesicles.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Brain - metabolism</subject><subject>Caenorhabditis elegans</subject><subject>Caenorhabditis elegans - chemistry</subject><subject>Caenorhabditis elegans Proteins</subject><subject>Caenorhabditis elegans UNC-17</subject><subject>Carrier Proteins - chemistry</subject><subject>Cloning, Molecular</subject><subject>Glycoproteins - chemistry</subject><subject>Helminth Proteins - chemistry</subject><subject>Marine</subject><subject>Membrane Glycoproteins</subject><subject>Membrane Transport Proteins</subject><subject>Molecular Sequence Data</subject><subject>Neuropeptides</subject><subject>Piperidines - metabolism</subject><subject>Receptors, Cholinergic - chemistry</subject><subject>Receptors, Cholinergic - genetics</subject><subject>Receptors, Cholinergic - metabolism</subject><subject>RNA, Messenger - genetics</subject><subject>RNA, Messenger - metabolism</subject><subject>Sequence Alignment</subject><subject>Sequence Homology, Amino Acid</subject><subject>Torpedo - metabolism</subject><subject>Torpedo electric lobe</subject><subject>Torpedo marmorata</subject><subject>Torpedo ocellata</subject><subject>Vesamicol</subject><subject>Vesicular Acetylcholine Transport Proteins</subject><subject>Vesicular acetylcholine transporter</subject><subject>Vesicular Biogenic Amine Transport Proteins</subject><subject>Vesicular Monoamine Transport Proteins</subject><subject>Vesicular Transport Proteins</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc-O0zAQxiMEWsrCG4DkE4JDwK7_c0BCEbBIK7gUaW-W40xbo8QOtlPoi_F8JG21RziNRvP7vtHMV1XPCX5DMBFvMSas5lLTV5q9VpjrdX33oFoRJWlNmVAPq9U98rh6kvMPPPeK6KvqShFGFVer6k_Tx-DDDtnQIfg9JsjZx4DiFpU9oANkO3gXe9T60C3cmGIBH9A2xeGEDDb5ACjZI9rENEIX36GbOMQ-7o7oly_7EzVOxRZ_ODl6N_U2IeugHHu3j_2iL8mGPMZUIKHvX5uayPOKxkKIaW_bzhefEfSwm8Gn1aOt7TM8u9TravPp46a5qW-_ff7SfLitHaWy1K4jruPYMtaJlmLsuOatVowK1WIllXbCWUzdltt1S-h6DZIqybUDEFZrel29PNvOV_-cIBcz-Oyg722AOGUjBSOUS_FfkAiBCRdyBtkZdCnmnGBrxuTnFx4NwWaJ1SyZmSUzo5k5xWruZtmLi__UDtDdiy45zvP35znMzzh4SCY7D8FB5xO4Yrro_73gL5wvteo</recordid><startdate>19940328</startdate><enddate>19940328</enddate><creator>Varoqui, Hélène</creator><creator>Diebler, Marie-Françoise</creator><creator>Meunier, François-Marie</creator><creator>Rand, James B.</creator><creator>Usdin, Ted B.</creator><creator>Bonner, Tom I.</creator><creator>Eiden, Lee E.</creator><creator>Erickson, Jeffrey D.</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>8FD</scope><scope>F1W</scope><scope>FR3</scope><scope>H95</scope><scope>H99</scope><scope>L.F</scope><scope>L.G</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19940328</creationdate><title>Cloning and expression of the vesamicol binding protein from the marine ray Torpedo: Homology with the putative vesicular acetylcholine transporter UNC-17 from Caenorhabditis elegans</title><author>Varoqui, Hélène ; Diebler, Marie-Françoise ; Meunier, François-Marie ; Rand, James B. ; Usdin, Ted B. ; Bonner, Tom I. ; Eiden, Lee E. ; Erickson, Jeffrey D.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c337t-cd1cd50a44d6b300c595b984368b08789c6ca03cf5a2b1322e738759cee6a993</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Brain - metabolism</topic><topic>Caenorhabditis elegans</topic><topic>Caenorhabditis elegans - chemistry</topic><topic>Caenorhabditis elegans Proteins</topic><topic>Caenorhabditis elegans UNC-17</topic><topic>Carrier Proteins - chemistry</topic><topic>Cloning, Molecular</topic><topic>Glycoproteins - chemistry</topic><topic>Helminth Proteins - chemistry</topic><topic>Marine</topic><topic>Membrane Glycoproteins</topic><topic>Membrane Transport Proteins</topic><topic>Molecular Sequence Data</topic><topic>Neuropeptides</topic><topic>Piperidines - metabolism</topic><topic>Receptors, Cholinergic - chemistry</topic><topic>Receptors, Cholinergic - genetics</topic><topic>Receptors, Cholinergic - metabolism</topic><topic>RNA, Messenger - genetics</topic><topic>RNA, Messenger - metabolism</topic><topic>Sequence Alignment</topic><topic>Sequence Homology, Amino Acid</topic><topic>Torpedo - metabolism</topic><topic>Torpedo electric lobe</topic><topic>Torpedo marmorata</topic><topic>Torpedo ocellata</topic><topic>Vesamicol</topic><topic>Vesicular Acetylcholine Transport Proteins</topic><topic>Vesicular acetylcholine transporter</topic><topic>Vesicular Biogenic Amine Transport Proteins</topic><topic>Vesicular Monoamine Transport Proteins</topic><topic>Vesicular Transport Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Varoqui, Hélène</creatorcontrib><creatorcontrib>Diebler, Marie-Françoise</creatorcontrib><creatorcontrib>Meunier, François-Marie</creatorcontrib><creatorcontrib>Rand, James B.</creatorcontrib><creatorcontrib>Usdin, Ted B.</creatorcontrib><creatorcontrib>Bonner, Tom I.</creatorcontrib><creatorcontrib>Eiden, Lee E.</creatorcontrib><creatorcontrib>Erickson, Jeffrey D.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Engineering Research Database</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>ASFA: Marine Biotechnology Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Marine Biotechnology Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Varoqui, Hélène</au><au>Diebler, Marie-Françoise</au><au>Meunier, François-Marie</au><au>Rand, James B.</au><au>Usdin, Ted B.</au><au>Bonner, Tom I.</au><au>Eiden, Lee E.</au><au>Erickson, Jeffrey D.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cloning and expression of the vesamicol binding protein from the marine ray Torpedo: Homology with the putative vesicular acetylcholine transporter UNC-17 from Caenorhabditis elegans</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1994-03-28</date><risdate>1994</risdate><volume>342</volume><issue>1</issue><spage>97</spage><epage>102</epage><pages>97-102</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>Complementary DNA clones corresponding to a messenger RNA encoding a 56 kDa polypeptide have been obtained from
Torpedo marmorata and
Torpedo ocellata electric lobe libraries, by homology screening with a probe obtained from the putative acetylcholine transporter from the nematode
Caenorhabditis elegans. The
Torpedo proteins display approximately 50% overall identity to the
C. elegans unc-17 protein and 43% identity to the two vesicle monoamine transporters (VMAT1 and VMAT2). This family of proteins is highly conserved within 12 domains which potentially span the vesicle membrane, with little similarity within the putative intraluminal glycosylated loop and at the N- and C-termini. The ~ 3.0 kb mRNA species is specifically expressed in the brain and highly enriched in the electric lobe of
Torpedo. The
Torpedo protein, expressed in CV-1 fibroblast cells, possesses a high-affinity binding site for vesamicol (
K
d = 6 nM), a drug which blocks in vitro and in vivo acetylcholine accumulation in cholinergic vesicles.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>8143858</pmid><doi>10.1016/0014-5793(94)80592-X</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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ispartof | FEBS letters, 1994-03, Vol.342 (1), p.97-102 |
issn | 0014-5793 1873-3468 |
language | eng |
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source | MEDLINE; Elsevier ScienceDirect Journals; Alma/SFX Local Collection; EZB Electronic Journals Library |
subjects | Amino Acid Sequence Animals Base Sequence Brain - metabolism Caenorhabditis elegans Caenorhabditis elegans - chemistry Caenorhabditis elegans Proteins Caenorhabditis elegans UNC-17 Carrier Proteins - chemistry Cloning, Molecular Glycoproteins - chemistry Helminth Proteins - chemistry Marine Membrane Glycoproteins Membrane Transport Proteins Molecular Sequence Data Neuropeptides Piperidines - metabolism Receptors, Cholinergic - chemistry Receptors, Cholinergic - genetics Receptors, Cholinergic - metabolism RNA, Messenger - genetics RNA, Messenger - metabolism Sequence Alignment Sequence Homology, Amino Acid Torpedo - metabolism Torpedo electric lobe Torpedo marmorata Torpedo ocellata Vesamicol Vesicular Acetylcholine Transport Proteins Vesicular acetylcholine transporter Vesicular Biogenic Amine Transport Proteins Vesicular Monoamine Transport Proteins Vesicular Transport Proteins |
title | Cloning and expression of the vesamicol binding protein from the marine ray Torpedo: Homology with the putative vesicular acetylcholine transporter UNC-17 from Caenorhabditis elegans |
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