Complete mRNA Coding Sequence of the Acetylcholine Binding α -Subunit of Torpedo marmorata Acetylcholine Receptor: A Model for the Transmembrane Organization of the Polypeptide Chain
A 1,350-base-pair-long cDNA clone, named pα -2, was isolated by hybridization to the previously characterized clone pα -1 and found to be specific for the α -subunit of the Torpedo marmorata acetylcholine receptor. The nucleotide sequences of both cDNA inserts were analyzed and the sequence of the c...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1983-04, Vol.80 (7), p.2067-2071 |
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| container_end_page | 2071 |
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| container_issue | 7 |
| container_start_page | 2067 |
| container_title | Proceedings of the National Academy of Sciences - PNAS |
| container_volume | 80 |
| creator | Devillers-Thiery, Anne Giraudat, Jerome Bentaboulet, Martine Changeux, Jean-Pierre |
| description | A 1,350-base-pair-long cDNA clone, named pα -2, was isolated by hybridization to the previously characterized clone pα -1 and found to be specific for the α -subunit of the Torpedo marmorata acetylcholine receptor. The nucleotide sequences of both cDNA inserts were analyzed and the sequence of the complete coding region and part of the 5′and 3′untranslated regions of the α -chain mRNA was determined. The complete amino acid sequence of the α -chain precursor is presented and used to develop a model for the transmembrane organization of the polypeptide. |
| doi_str_mv | 10.1073/pnas.80.7.2067 |
| format | Article |
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The nucleotide sequences of both cDNA inserts were analyzed and the sequence of the complete coding region and part of the 5′and 3′untranslated regions of the α -chain mRNA was determined. 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The complete amino acid sequence of the α -chain precursor is presented and used to develop a model for the transmembrane organization of the polypeptide.</description><subject>acetylcholine</subject><subject>Acetylcholine - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Binding Sites</subject><subject>Complementary DNA</subject><subject>DNA</subject><subject>Generally accepted auditing standards</subject><subject>Macromolecular Substances</subject><subject>Marine</subject><subject>Membrane Proteins - genetics</subject><subject>membranes</subject><subject>Messenger RNA</subject><subject>Models, Biological</subject><subject>mRNA</subject><subject>neurophysiology</subject><subject>nucleotide sequence</subject><subject>Nucleotide sequences</subject><subject>Nucleotides</subject><subject>P branes</subject><subject>Protein Conformation</subject><subject>Receptors, Cholinergic - genetics</subject><subject>RNA</subject><subject>RNA, Messenger - genetics</subject><subject>String theory</subject><subject>Synaptic Membranes - ultrastructure</subject><subject>Torpedo</subject><subject>Torpedo marmorata</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1983</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFks2O0zAUhSMEGsrAlgUSklfsWmzHiRMkFqXiTxoYNFPWluPcth45dsZ2EOWtWPEWPBPOtFMKQmLlxTnf8b32ybLHBM8I5vnz3sowq_CMzygu-Z1sQnBNpiWr8d1sgjHl04pRdj97EMIVxrguKnySnZQFp3VJJ9mPhet6AxFQd_Fxjhau1XaNLuF6AKsAuRWKG0BzBXFr1MYZbQG90vbG9fM7ml4OzWB1HI1L53toHeqk75yXUf6FXYCCPjr_As3RB9eCQSvnb-KXXtrQQdekE9C5X0urv8monb0d4JMz2z7RugW02EhtH2b3VtIEeLQ_T7PPb14vF--mZ-dv3y_mZ1PFcpJ2lxUtqgJU3tIGOFcNpkQpSSvJGC8p4Jo1HLdSqrKUBS8aQpniLa_JiJb5afZyl9sPTQetAhu9NKL3Oq25FU5q8adi9Uas3ReR1zkvWOKf7Xnv0puGKDodFBiTNnVDEBVmtGSE_NdI8qKqClYn42xnVN6F4GF1GIZgMVZCjJVIwYKLsRIJeHq8wsG-78DRzSN3qx54sRqMifA1HgX905j0Jzv9KqRv_j1WznKe_wIoLddc</recordid><startdate>19830401</startdate><enddate>19830401</enddate><creator>Devillers-Thiery, Anne</creator><creator>Giraudat, Jerome</creator><creator>Bentaboulet, Martine</creator><creator>Changeux, Jean-Pierre</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><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>7TK</scope><scope>7TM</scope><scope>8FD</scope><scope>F1W</scope><scope>FR3</scope><scope>H95</scope><scope>L.G</scope><scope>M7Z</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19830401</creationdate><title>Complete mRNA Coding Sequence of the Acetylcholine Binding α -Subunit of Torpedo marmorata Acetylcholine Receptor: A Model for the Transmembrane Organization of the Polypeptide Chain</title><author>Devillers-Thiery, Anne ; Giraudat, Jerome ; Bentaboulet, Martine ; Changeux, Jean-Pierre</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4317-8a82585ec3d2be77cb021cca28a44762e094b70daac66a575b124c7d7918a8263</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1983</creationdate><topic>acetylcholine</topic><topic>Acetylcholine - metabolism</topic><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Binding Sites</topic><topic>Complementary DNA</topic><topic>DNA</topic><topic>Generally accepted auditing standards</topic><topic>Macromolecular Substances</topic><topic>Marine</topic><topic>Membrane Proteins - genetics</topic><topic>membranes</topic><topic>Messenger RNA</topic><topic>Models, Biological</topic><topic>mRNA</topic><topic>neurophysiology</topic><topic>nucleotide sequence</topic><topic>Nucleotide sequences</topic><topic>Nucleotides</topic><topic>P branes</topic><topic>Protein Conformation</topic><topic>Receptors, Cholinergic - genetics</topic><topic>RNA</topic><topic>RNA, Messenger - genetics</topic><topic>String theory</topic><topic>Synaptic Membranes - ultrastructure</topic><topic>Torpedo</topic><topic>Torpedo marmorata</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Devillers-Thiery, Anne</creatorcontrib><creatorcontrib>Giraudat, Jerome</creatorcontrib><creatorcontrib>Bentaboulet, Martine</creatorcontrib><creatorcontrib>Changeux, Jean-Pierre</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</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>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>Biochemistry Abstracts 1</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Devillers-Thiery, Anne</au><au>Giraudat, Jerome</au><au>Bentaboulet, Martine</au><au>Changeux, Jean-Pierre</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Complete mRNA Coding Sequence of the Acetylcholine Binding α -Subunit of Torpedo marmorata Acetylcholine Receptor: A Model for the Transmembrane Organization of the Polypeptide Chain</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1983-04-01</date><risdate>1983</risdate><volume>80</volume><issue>7</issue><spage>2067</spage><epage>2071</epage><pages>2067-2071</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>A 1,350-base-pair-long cDNA clone, named pα -2, was isolated by hybridization to the previously characterized clone pα -1 and found to be specific for the α -subunit of the Torpedo marmorata acetylcholine receptor. The nucleotide sequences of both cDNA inserts were analyzed and the sequence of the complete coding region and part of the 5′and 3′untranslated regions of the α -chain mRNA was determined. The complete amino acid sequence of the α -chain precursor is presented and used to develop a model for the transmembrane organization of the polypeptide.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>6572962</pmid><doi>10.1073/pnas.80.7.2067</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
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| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1983-04, Vol.80 (7), p.2067-2071 |
| issn | 0027-8424 1091-6490 |
| language | eng |
| recordid | cdi_pubmed_primary_6572962 |
| source | Jstor Complete Legacy; MEDLINE; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | acetylcholine Acetylcholine - metabolism Amino Acid Sequence Amino acids Animals Base Sequence Binding Sites Complementary DNA DNA Generally accepted auditing standards Macromolecular Substances Marine Membrane Proteins - genetics membranes Messenger RNA Models, Biological mRNA neurophysiology nucleotide sequence Nucleotide sequences Nucleotides P branes Protein Conformation Receptors, Cholinergic - genetics RNA RNA, Messenger - genetics String theory Synaptic Membranes - ultrastructure Torpedo Torpedo marmorata |
| title | Complete mRNA Coding Sequence of the Acetylcholine Binding α -Subunit of Torpedo marmorata Acetylcholine Receptor: A Model for the Transmembrane Organization of the Polypeptide Chain |
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