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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1995-2-23
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pubmed:databankReference | |
pubmed:abstractText |
In order to characterize individual protein components of the mitochondrial (mt) ribosome for regulatory, functional and evolutionary studies, the yeast nuclear gene MRP-L4 (accession No. Z30582), coding for the mt ribosomal protein (MRP) YmL4, has been cloned using oligodeoxyribonucleotides (oligos) deduced from a partial amino acid (aa) sequence [Graack et al., FEBS Lett. 242 (1988) 4-8] as screening probes. MRP-L4 is located on chromosome XII and codes for a slightly basic protein of 319 aa. The first 14 aa have not been found in the mature protein, and putatively form a signal peptide that is cleaved off during or after mt import. YmL4 has an N terminus very rich in Pro residues, and at its C terminus contains four hydrophobic domains. YmL4 shows no significant sequence similarity to any other sequence from the databases. Gene disruption shows the MRP-L4 product to be indispensable for mt function in cells growing on non-fermentable carbon sources. In contrast to nearly all other MRPs investigated so far, gene disruption of MRP-L4 also affects growth of yeast cells on fermentable carbon sources, suggesting additional cytosolic and/or mt functions of YmL4 besides its involvement in mt protein biosynthesis.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Mitochondrial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Sorting Signals,
http://linkedlifedata.com/resource/pubmed/chemical/Ribosomal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0378-1119
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
11
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pubmed:volume |
152
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pubmed:geneSymbol |
MRP-L4
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
107-12
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:7828914-Amino Acid Sequence,
pubmed-meshheading:7828914-Base Sequence,
pubmed-meshheading:7828914-Cell Compartmentation,
pubmed-meshheading:7828914-Chromosomes, Fungal,
pubmed-meshheading:7828914-Cloning, Molecular,
pubmed-meshheading:7828914-Genes, Fungal,
pubmed-meshheading:7828914-Genes, Lethal,
pubmed-meshheading:7828914-Mitochondria,
pubmed-meshheading:7828914-Mitochondrial Proteins,
pubmed-meshheading:7828914-Molecular Sequence Data,
pubmed-meshheading:7828914-Mutagenesis, Insertional,
pubmed-meshheading:7828914-Protein Sorting Signals,
pubmed-meshheading:7828914-Ribosomal Proteins,
pubmed-meshheading:7828914-Saccharomyces cerevisiae,
pubmed-meshheading:7828914-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:7828914-Sequence Analysis, DNA,
pubmed-meshheading:7828914-Sequence Homology, Amino Acid
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pubmed:year |
1995
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pubmed:articleTitle |
Gene MRP-L4, encoding mitochondrial ribosomal protein YmL4, is indispensable for proper non-respiratory cell functions in yeast.
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pubmed:affiliation |
Institut für Genetik, Freie Universität Berlin, Germany.
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pubmed:publicationType |
Journal Article,
Comparative Study
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