A protein required for splicing group I introns in Neurospora mitochondria is mitochondrial tyrosyl-tRNA synthetase or a derivative thereof
Identifieur interne : 004D07 ( Main/Exploration ); précédent : 004D06; suivant : 004D08A protein required for splicing group I introns in Neurospora mitochondria is mitochondrial tyrosyl-tRNA synthetase or a derivative thereof
Auteurs : Robert A. Akins [États-Unis] ; Alan M. Lambowitz [États-Unis]Source :
- Cell [ 0092-8674 ] ; 1987.
English descriptors
- Teeft :
- Acad, Akins, Amino, Amino acid, Amino acids, Aminoacylation, Assay, Bacterial synthetases, Bacteriophage, Bertrand, Biol, Cech, Clone, Coli, Column fractions, Crassa, Cytochrome, Different group, Encodes, Experimental procedures, Garriga, Gene, Gene encodes, Gene encodes mitochondrial synthetase, Gene product, Homology, Intron, Lambowitz, Minimal medium, Mitochondrial, Mitochondrial lysates, Mitochondrial protein synthesis, Mitochondrial rnps, Mitochondrial synthetase, Mitochondrial synthetase activity, Mitochondrial synthetases, Mitochondrial tyrosyltrna synthetase, Mitochondrion, Mtdna, Mtdna introns, Mutant, Mutation, Natl, Neurospora, Neurospora chromosomal, Neurospora crassa, Neurospora mitochondria, Neurospora mitochondrial, Neurospora protein, Nuclear mutants, Nuclease, Oeql, Open reading frame, Partial revertants, Pellet, Phosphocellulose, Plasmid, Plasmid pral1, Polypeptide, Pral1, Proc, Raql, Reading frame, Restriction fragments, Revertants, Rna, Rnps, Rrna, Rrna intron, Saccharomyces cerevisiae, Salllhindlll, Salllhindlll fragment, Sequencing, Significant homology, Soluble activity, Splice site, Synthetase, Synthetase activities, Synthetases, Tetrahymena, Transformants, Trna, Tzagoloff, Unpublished data, Yeast.
Abstract
Abstract: The nuclear cyt-18 mutants of Neurospora crassa are defective in splicing a number of group I introns in mitochondria. Here, cloning and sequencing of the cyt-18 gene show that it contains an open reading frame having significant homology to bacterial tyrosyl-tRNA synthetases. Biochemical and genetic experiments lead to the conclusions that the cyt-18 gene encodes mitochondrial tyrosyl-tRNA synthetase, that mutations in this gene inhibit splicing directly, and that mitochondrial tyrosyl-tRNA synthetase or a derivative of this protein is related to the soluble activity that functions in splicing the mitochondrial large rRNA intron and possibly other group I introns. Analysis of partial revertants provides direct evidence that the cyt-18 gene encodes a protein or proteins with two activities, splicing and aminoacylation, that can be partially separated by mutation. Our findings may be relevant to the evolution of introns and splicing mechanisms in eukaryotes.
Url:
DOI: 10.1016/0092-8674(87)90488-0
Affiliations:
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Lambowitz</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Ohio</region></placeName><wicri:cityArea>Department of Molecular Genetics The Ohio State University Columbus</wicri:cityArea></affiliation><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Ohio</region></placeName><wicri:cityArea>Department of Biochemistry The Ohio State University Columbus</wicri:cityArea></affiliation></author></analytic><monogr></monogr><series><title level="j">Cell</title><title level="j" type="abbrev">CELL</title><idno type="ISSN">0092-8674</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1987">1987</date><biblScope unit="volume">50</biblScope><biblScope unit="issue">3</biblScope><biblScope unit="page" from="331">331</biblScope><biblScope unit="page" to="345">345</biblScope></imprint><idno type="ISSN">0092-8674</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0092-8674</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Acad</term><term>Akins</term><term>Amino</term><term>Amino acid</term><term>Amino acids</term><term>Aminoacylation</term><term>Assay</term><term>Bacterial synthetases</term><term>Bacteriophage</term><term>Bertrand</term><term>Biol</term><term>Cech</term><term>Clone</term><term>Coli</term><term>Column fractions</term><term>Crassa</term><term>Cytochrome</term><term>Different group</term><term>Encodes</term><term>Experimental procedures</term><term>Garriga</term><term>Gene</term><term>Gene encodes</term><term>Gene encodes mitochondrial synthetase</term><term>Gene product</term><term>Homology</term><term>Intron</term><term>Lambowitz</term><term>Minimal medium</term><term>Mitochondrial</term><term>Mitochondrial lysates</term><term>Mitochondrial protein synthesis</term><term>Mitochondrial rnps</term><term>Mitochondrial synthetase</term><term>Mitochondrial synthetase activity</term><term>Mitochondrial synthetases</term><term>Mitochondrial tyrosyltrna synthetase</term><term>Mitochondrion</term><term>Mtdna</term><term>Mtdna introns</term><term>Mutant</term><term>Mutation</term><term>Natl</term><term>Neurospora</term><term>Neurospora chromosomal</term><term>Neurospora crassa</term><term>Neurospora mitochondria</term><term>Neurospora mitochondrial</term><term>Neurospora protein</term><term>Nuclear mutants</term><term>Nuclease</term><term>Oeql</term><term>Open reading frame</term><term>Partial revertants</term><term>Pellet</term><term>Phosphocellulose</term><term>Plasmid</term><term>Plasmid pral1</term><term>Polypeptide</term><term>Pral1</term><term>Proc</term><term>Raql</term><term>Reading frame</term><term>Restriction fragments</term><term>Revertants</term><term>Rna</term><term>Rnps</term><term>Rrna</term><term>Rrna intron</term><term>Saccharomyces cerevisiae</term><term>Salllhindlll</term><term>Salllhindlll fragment</term><term>Sequencing</term><term>Significant homology</term><term>Soluble activity</term><term>Splice site</term><term>Synthetase</term><term>Synthetase activities</term><term>Synthetases</term><term>Tetrahymena</term><term>Transformants</term><term>Trna</term><term>Tzagoloff</term><term>Unpublished data</term><term>Yeast</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The nuclear cyt-18 mutants of Neurospora crassa are defective in splicing a number of group I introns in mitochondria. Here, cloning and sequencing of the cyt-18 gene show that it contains an open reading frame having significant homology to bacterial tyrosyl-tRNA synthetases. Biochemical and genetic experiments lead to the conclusions that the cyt-18 gene encodes mitochondrial tyrosyl-tRNA synthetase, that mutations in this gene inhibit splicing directly, and that mitochondrial tyrosyl-tRNA synthetase or a derivative of this protein is related to the soluble activity that functions in splicing the mitochondrial large rRNA intron and possibly other group I introns. Analysis of partial revertants provides direct evidence that the cyt-18 gene encodes a protein or proteins with two activities, splicing and aminoacylation, that can be partially separated by mutation. Our findings may be relevant to the evolution of introns and splicing mechanisms in eukaryotes.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Ohio</li></region></list><tree><country name="États-Unis"><region name="Ohio"><name sortKey="Akins, Robert A" sort="Akins, Robert A" uniqKey="Akins R" first="Robert A." last="Akins">Robert A. Akins</name></region><name sortKey="Akins, Robert A" sort="Akins, Robert A" uniqKey="Akins R" first="Robert A." last="Akins">Robert A. Akins</name><name sortKey="Lambowitz, Alan M" sort="Lambowitz, Alan M" uniqKey="Lambowitz A" first="Alan M." last="Lambowitz">Alan M. Lambowitz</name><name sortKey="Lambowitz, Alan M" sort="Lambowitz, Alan M" uniqKey="Lambowitz A" first="Alan M." last="Lambowitz">Alan M. Lambowitz</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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