Isolation and sequence of cDNA clones coding for the precursor to the γ subunit of mouse muscle nicotinic acetylcholine receptor
Identifieur interne : 002241 ( Istex/Checkpoint ); précédent : 002240; suivant : 002242Isolation and sequence of cDNA clones coding for the precursor to the γ subunit of mouse muscle nicotinic acetylcholine receptor
Auteurs : J. Boulter [États-Unis] ; K. Evans [États-Unis] ; G. Martin [États-Unis] ; P. Mason [États-Unis] ; S. Stengelin [États-Unis] ; D. Goldman [États-Unis] ; S. Heinemann [États-Unis] ; J. Patrick [États-Unis]Source :
- Journal of Neuroscience Research [ 0360-4012 ] ; 1986.
English descriptors
- Teeft :
- Aataaa, Acad, Acetylcholine, Acetylcholine receptor, Acetylcholine receptor clones, Amino, Amino acid homology, Amino acid sequence, Amino acid sequences, Amino acids, Biol, Boulter, Cdna, Cdna clones coding, Cdna libraries, Chick, Clone, Coding, Denervated, Denervated mouse limb muscle, Different lengths, Dscdna, Goldman, Heinemann, Homology, Human acetylcholine receptor, Hybridization, Mature protein, Mouse acetylcholine receptor, Mouse brain, Mouse muscle acetylcholine receptor, Mouse muscle nicotinic acetylcholine receptor, Mrna, Natl, Negative numbers, Neural regulation, Nicotinic, Nicotinic acetylcholine receptor, Noda, Nonfusing muscle cell line, Nucleic acids, Nucleotide, Nucleotide sequence, Numa, Peptide, Plasmid, Plasmid vector, Poly, Polyadenylation, Precursor, Primary structure, Proc, Proc natl acad, Receptor, Rna, Sequencing, Signal peptide, Sspe, Subunit, Subunit mrna, Subunit poly, Takahashi, Takai.
Abstract
cDNA libraries have been constructed in plasmid (pBR322) and bacteriophage (λgt10) vectors with poly (A +) RNA isolated from the nonfusing mouse muscle cell line BC3H‐1. The libraries were screened with a restriction fragment derived from a genomic clone coding for a human acetylcholine receptor γ subunit. Several clones were obtained whose cDNA inserts possessed nucleotide and deduced amino acid sequence homology with acetylcholine receptor γ subunits from Torpedo californica, chick, calf, and human. One isolate, λBMG419, has 88 nucleotides of 5′‐untranslated sequence, an open reading frame of 1,557 nucleotides coding for the precursor to the mouse acetylcholine receptor γ subunit, and 144 nucleotides of 3′‐untranslated sequence. Alignment of the λBMG419‐deduced amino acid sequence with homologs from other species predicts a precursor peptide of 519 amino acids and a mature protein of 497 amino acids, with nonglycosylated molecular weights of 58,744 and 56,424 daltons, respectively. Comparison of the deduced amino acid sequence of the mouse γ subunit with Torpedo, chick, calf, and human sequences showed overall homologies of 54%, 67%, 90%, and 90%, respectively; however, significantly higher homologies were found in several putative functional domains. Radiolabeled λBMG419 has been used to identify homologous RNA species, one of approximately 2 kb and one of about 3.5 kb, in poly (A +) RNA prepared from BC3H‐1 cells and denervated mouse limb muscle. γ Subunit‐coding RNA species are considerably more abundant in denervated than in innervated muscle, suggesting that neural regulation of the abundance of theγ subunit is exerted through regulation of the amount of its mRNA.
Url:
DOI: 10.1002/jnr.490160106
Affiliations:
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Goldman</name></author><author><name sortKey="Heinemann, S" sort="Heinemann, S" uniqKey="Heinemann S" first="S." last="Heinemann">S. Heinemann</name></author><author><name sortKey="Patrick, J" sort="Patrick, J" uniqKey="Patrick J" first="J." last="Patrick">J. 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Boulter</name><affiliation wicri:level="2"><country>États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>Molecular Neurobiology Laboratory, The Salk Institute, San Diego</wicri:cityArea></affiliation><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>Correspondence address: Molecular Neurobiology Laboratory, The Salk Institute, San Diego</wicri:cityArea></affiliation></author><author><name sortKey="Evans, K" sort="Evans, K" uniqKey="Evans K" first="K." last="Evans">K. Evans</name><affiliation wicri:level="2"><country>États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>Molecular Neurobiology Laboratory, The Salk Institute, San Diego</wicri:cityArea></affiliation></author><author><name sortKey="Martin, G" sort="Martin, G" uniqKey="Martin G" first="G." last="Martin">G. Martin</name><affiliation wicri:level="2"><country>États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>Molecular Neurobiology Laboratory, The Salk Institute, San Diego</wicri:cityArea></affiliation></author><author><name sortKey="Mason, P" sort="Mason, P" uniqKey="Mason P" first="P." last="Mason">P. Mason</name><affiliation wicri:level="2"><country>États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>Molecular Neurobiology Laboratory, The Salk Institute, San Diego</wicri:cityArea></affiliation></author><author><name sortKey="Stengelin, S" sort="Stengelin, S" uniqKey="Stengelin S" first="S." last="Stengelin">S. Stengelin</name><affiliation wicri:level="2"><country>États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>Molecular Neurobiology Laboratory, The Salk Institute, San Diego</wicri:cityArea></affiliation></author><author><name sortKey="Goldman, D" sort="Goldman, D" uniqKey="Goldman D" first="D." last="Goldman">D. Goldman</name><affiliation wicri:level="2"><country>États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>Molecular Neurobiology Laboratory, The Salk Institute, San Diego</wicri:cityArea></affiliation></author><author><name sortKey="Heinemann, S" sort="Heinemann, S" uniqKey="Heinemann S" first="S." last="Heinemann">S. Heinemann</name><affiliation wicri:level="2"><country>États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>Molecular Neurobiology Laboratory, The Salk Institute, San Diego</wicri:cityArea></affiliation></author><author><name sortKey="Patrick, J" sort="Patrick, J" uniqKey="Patrick J" first="J." last="Patrick">J. Patrick</name><affiliation wicri:level="2"><country>États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>Molecular Neurobiology Laboratory, The Salk Institute, San Diego</wicri:cityArea></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">Journal of Neuroscience Research</title><title level="j" type="alt">JOURNAL OF NEUROSCIENCE RESEARCH</title><idno type="ISSN">0360-4012</idno><idno type="eISSN">1097-4547</idno><imprint><biblScope unit="vol">16</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="37">37</biblScope><biblScope unit="page" to="49">49</biblScope><biblScope unit="page-count">13</biblScope><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>Hoboken</pubPlace><date type="published" when="1986">1986</date></imprint><idno type="ISSN">0360-4012</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0360-4012</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Aataaa</term><term>Acad</term><term>Acetylcholine</term><term>Acetylcholine receptor</term><term>Acetylcholine receptor clones</term><term>Amino</term><term>Amino acid homology</term><term>Amino acid sequence</term><term>Amino acid sequences</term><term>Amino acids</term><term>Biol</term><term>Boulter</term><term>Cdna</term><term>Cdna clones coding</term><term>Cdna libraries</term><term>Chick</term><term>Clone</term><term>Coding</term><term>Denervated</term><term>Denervated mouse limb muscle</term><term>Different lengths</term><term>Dscdna</term><term>Goldman</term><term>Heinemann</term><term>Homology</term><term>Human acetylcholine receptor</term><term>Hybridization</term><term>Mature protein</term><term>Mouse acetylcholine receptor</term><term>Mouse brain</term><term>Mouse muscle acetylcholine receptor</term><term>Mouse muscle nicotinic acetylcholine receptor</term><term>Mrna</term><term>Natl</term><term>Negative numbers</term><term>Neural regulation</term><term>Nicotinic</term><term>Nicotinic acetylcholine receptor</term><term>Noda</term><term>Nonfusing muscle cell line</term><term>Nucleic acids</term><term>Nucleotide</term><term>Nucleotide sequence</term><term>Numa</term><term>Peptide</term><term>Plasmid</term><term>Plasmid vector</term><term>Poly</term><term>Polyadenylation</term><term>Precursor</term><term>Primary structure</term><term>Proc</term><term>Proc natl acad</term><term>Receptor</term><term>Rna</term><term>Sequencing</term><term>Signal peptide</term><term>Sspe</term><term>Subunit</term><term>Subunit mrna</term><term>Subunit poly</term><term>Takahashi</term><term>Takai</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">cDNA libraries have been constructed in plasmid (pBR322) and bacteriophage (λgt10) vectors with poly (A +) RNA isolated from the nonfusing mouse muscle cell line BC3H‐1. The libraries were screened with a restriction fragment derived from a genomic clone coding for a human acetylcholine receptor γ subunit. Several clones were obtained whose cDNA inserts possessed nucleotide and deduced amino acid sequence homology with acetylcholine receptor γ subunits from Torpedo californica, chick, calf, and human. One isolate, λBMG419, has 88 nucleotides of 5′‐untranslated sequence, an open reading frame of 1,557 nucleotides coding for the precursor to the mouse acetylcholine receptor γ subunit, and 144 nucleotides of 3′‐untranslated sequence. Alignment of the λBMG419‐deduced amino acid sequence with homologs from other species predicts a precursor peptide of 519 amino acids and a mature protein of 497 amino acids, with nonglycosylated molecular weights of 58,744 and 56,424 daltons, respectively. Comparison of the deduced amino acid sequence of the mouse γ subunit with Torpedo, chick, calf, and human sequences showed overall homologies of 54%, 67%, 90%, and 90%, respectively; however, significantly higher homologies were found in several putative functional domains. Radiolabeled λBMG419 has been used to identify homologous RNA species, one of approximately 2 kb and one of about 3.5 kb, in poly (A +) RNA prepared from BC3H‐1 cells and denervated mouse limb muscle. γ Subunit‐coding RNA species are considerably more abundant in denervated than in innervated muscle, suggesting that neural regulation of the abundance of theγ subunit is exerted through regulation of the amount of its mRNA.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Californie</li></region></list><tree><country name="États-Unis"><region name="Californie"><name sortKey="Boulter, J" sort="Boulter, J" uniqKey="Boulter J" first="J." last="Boulter">J. Boulter</name></region><name sortKey="Boulter, J" sort="Boulter, J" uniqKey="Boulter J" first="J." last="Boulter">J. Boulter</name><name sortKey="Evans, K" sort="Evans, K" uniqKey="Evans K" first="K." last="Evans">K. Evans</name><name sortKey="Goldman, D" sort="Goldman, D" uniqKey="Goldman D" first="D." last="Goldman">D. Goldman</name><name sortKey="Heinemann, S" sort="Heinemann, S" uniqKey="Heinemann S" first="S." last="Heinemann">S. Heinemann</name><name sortKey="Martin, G" sort="Martin, G" uniqKey="Martin G" first="G." last="Martin">G. Martin</name><name sortKey="Mason, P" sort="Mason, P" uniqKey="Mason P" first="P." last="Mason">P. Mason</name><name sortKey="Patrick, J" sort="Patrick, J" uniqKey="Patrick J" first="J." last="Patrick">J. Patrick</name><name sortKey="Stengelin, S" sort="Stengelin, S" uniqKey="Stengelin S" first="S." last="Stengelin">S. Stengelin</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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