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http://purl.uniprot.org/citations/4580557http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/4580557http://www.w3.org/2000/01/rdf-schema#comment"The effects of mutations occurring at three independent loci, eth2, eth3, and eth10, were studied on the basis of several criteria: level of resistance towards two methionine analogues (ethionine and selenomethionine), pool sizes of free methionine and S-adenosyl methionine (SAM) under different growth conditions, and susceptibility towards methionine-mediated repression and SAM-mediated repression of some enzymes involved in methionine biosynthesis (met group I enzymes). It was shown that: (i) the level of resistance towards both methionine analogues roughly correlates with the amount of methionine accumulated in the pool; (ii) the repressibility of met group I enzymes by exogenous methionine is either abolished or greatly lowered, depending upon the mutation studied; (iii) the repressibility of the same enzymes by exogenous SAM remains, in at least three mutants studied, close to that observed in a wild-type strain; (iv) the accumulation of SAM does not occur in the most extreme mutants either from endogenously overproduced or from exogenously supplied methionine: (v) the two methionine-activating enzymes, methionyl-transfer ribonucleic acid (tRNA) synthetase and methionine adenosyl transferase, do not seem modified in any of the mutants presented here; and (vi) the amount of tRNA(met) and its level of charging are alike in all strains. Thus, the three recessive mutations presented here affect methionine-mediated repression, both at the level of overall methionine biosynthesis which results in its accumulation in the pool, and at the level of the synthesis of met group I enzymes. The implications of these findings are discussed."xsd:string
http://purl.uniprot.org/citations/4580557http://purl.org/dc/terms/identifier"doi:10.1128/jb.115.3.1084-1093.1973"xsd:string
http://purl.uniprot.org/citations/4580557http://purl.uniprot.org/core/author"Cherest H."xsd:string
http://purl.uniprot.org/citations/4580557http://purl.uniprot.org/core/author"Surdin-Kerjan Y."xsd:string
http://purl.uniprot.org/citations/4580557http://purl.uniprot.org/core/author"de Robichon-Szulmajster H."xsd:string
http://purl.uniprot.org/citations/4580557http://purl.uniprot.org/core/author"Antoniewski J."xsd:string
http://purl.uniprot.org/citations/4580557http://purl.uniprot.org/core/date"1973"xsd:gYear
http://purl.uniprot.org/citations/4580557http://purl.uniprot.org/core/name"J Bacteriol"xsd:string
http://purl.uniprot.org/citations/4580557http://purl.uniprot.org/core/pages"1084-1093"xsd:string
http://purl.uniprot.org/citations/4580557http://purl.uniprot.org/core/title"Effects of regulatory mutations upon methionine biosynthesis in Saccharomyces cerevisiae: loci eth2-eth3-eth10."xsd:string
http://purl.uniprot.org/citations/4580557http://purl.uniprot.org/core/volume"115"xsd:string
http://purl.uniprot.org/citations/4580557http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/4580557
http://purl.uniprot.org/citations/4580557http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/4580557
http://purl.uniprot.org/uniprot/P10659#attribution-A2BA524A5A625880CD202DBE118D01B1http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/4580557
http://purl.uniprot.org/uniprot/#_P10659-mappedCitation-4580557http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/4580557
http://purl.uniprot.org/uniprot/P10659http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/4580557