RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/29343666http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/29343666http://www.w3.org/2000/01/rdf-schema#comment"Mitochondrial ribosomal protein L32 (MrpL32) of Saccharomyces cerevisiae is homologous to the bacterial L32 ribosomal protein. MrpL32 carries an N-terminal mitochondrion-targeting sequence (MTS) and is about 60 amino acid residues longer at the C-terminus. Adding to its function as a leader sequence, the MTS of MrpL32 has been reported to regulate ribosome biogenesis through its processing by m-AAA protease. However, the function of the C-terminal extension (CE) remains totally unknown. Therefore, we constructed a series of C-terminally truncated mrpl32 (mrpl32ΔC) genes and expressed them in a Δmrpl32 mutant to examine their function. Interestingly, some MrpL32ΔC derivatives exhibited temperature-sensitive (ts) growth on medium with non-fermentable carbon sources. Furthermore, the CE domain of MrpL32, expressed separately from MrpL32ΔC, could rescue the ts phenotype of mutants by improving mitochondrial protein synthesis."xsd:string
http://purl.uniprot.org/citations/29343666http://purl.org/dc/terms/identifier"doi:10.1266/ggs.17-00023"xsd:string
http://purl.uniprot.org/citations/29343666http://purl.uniprot.org/core/author"Kitakawa M."xsd:string
http://purl.uniprot.org/citations/29343666http://purl.uniprot.org/core/author"Woogeng I.N."xsd:string
http://purl.uniprot.org/citations/29343666http://purl.uniprot.org/core/date"2018"xsd:gYear
http://purl.uniprot.org/citations/29343666http://purl.uniprot.org/core/name"Genes Genet Syst"xsd:string
http://purl.uniprot.org/citations/29343666http://purl.uniprot.org/core/pages"21-24"xsd:string
http://purl.uniprot.org/citations/29343666http://purl.uniprot.org/core/title"The C-terminal extension domain of Saccharomyces cerevisiae MrpL32, a homolog of ribosomal protein L32, functions in trans to support mitochondrial translation."xsd:string
http://purl.uniprot.org/citations/29343666http://purl.uniprot.org/core/volume"93"xsd:string
http://purl.uniprot.org/citations/29343666http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/29343666
http://purl.uniprot.org/citations/29343666http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/29343666
http://purl.uniprot.org/uniprot/#_A0A8H4BTF4-mappedCitation-29343666http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/29343666
http://purl.uniprot.org/uniprot/#_P25348-mappedCitation-29343666http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/29343666
http://purl.uniprot.org/uniprot/A0A8H4BTF4http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/29343666
http://purl.uniprot.org/uniprot/P25348http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/29343666