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rdf:type |
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lifeskim:mentions |
umls-concept:C0010572,
umls-concept:C0033684,
umls-concept:C0035553,
umls-concept:C0205263,
umls-concept:C0220903,
umls-concept:C0332152,
umls-concept:C0683598,
umls-concept:C0812382,
umls-concept:C0997659,
umls-concept:C1334043,
umls-concept:C1514562
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pubmed:issue |
1
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pubmed:dateCreated |
2001-5-25
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pubmed:databankReference |
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pubmed:abstractText |
Cycloheximide (CYH) resistance in Candida maltosa is dependent on the induction of a ribosomal protein, Q-type L41, the 56th residue of which is glutamine, not proline as in ordinary P-type L41. We found that a 38-kDa protein in a wild-type C. maltosa ribosomal fraction became undetectable upon CYH treatment but detectable again with the establishment of CYH resistance by the induction of Q-type L41. We cloned a gene coding for this protein and named it RAY38 (ribosome-associated protein of yeast). Ray38p is a homolog of a purine motif triple-helical DNA-binding protein, Stm1p, and has a putative RNA-binding motif RGG. The ribosome-associated Ray38p was phosphorylated at serine and threonine residues, and Ray38p that was dissociated from ribosome by CYH treatment was highly phosphorylated in threonine residues. A ray38 null mutant recovered faster from CYH-caused growth stasis than the wild-type strain, suggesting that the dissociation of Ray38p from ribosome facilitates the induction of CYH resistance in C. maltosa.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cycloheximide,
http://linkedlifedata.com/resource/pubmed/chemical/Eukaryotic Initiation Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Initiation Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Synthesis Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/RNA Nucleotidyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Ribosomal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Serine,
http://linkedlifedata.com/resource/pubmed/chemical/TIF3 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Threonine
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0006-291X
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pubmed:author |
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pubmed:copyrightInfo |
Copyright 2001 Academic Press.
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
284
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
194-202
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11374890-Amino Acid Motifs,
pubmed-meshheading:11374890-Amino Acid Substitution,
pubmed-meshheading:11374890-Base Sequence,
pubmed-meshheading:11374890-Candida,
pubmed-meshheading:11374890-Cell Division,
pubmed-meshheading:11374890-Cycloheximide,
pubmed-meshheading:11374890-Eukaryotic Initiation Factors,
pubmed-meshheading:11374890-Fungal Proteins,
pubmed-meshheading:11374890-Molecular Sequence Data,
pubmed-meshheading:11374890-Molecular Weight,
pubmed-meshheading:11374890-Mutation,
pubmed-meshheading:11374890-Peptide Initiation Factors,
pubmed-meshheading:11374890-Phosphoproteins,
pubmed-meshheading:11374890-Phosphorylation,
pubmed-meshheading:11374890-Protein Binding,
pubmed-meshheading:11374890-Protein Synthesis Inhibitors,
pubmed-meshheading:11374890-RNA Nucleotidyltransferases,
pubmed-meshheading:11374890-Ribosomal Proteins,
pubmed-meshheading:11374890-Ribosomes,
pubmed-meshheading:11374890-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:11374890-Sequence Homology, Amino Acid,
pubmed-meshheading:11374890-Serine,
pubmed-meshheading:11374890-Subcellular Fractions,
pubmed-meshheading:11374890-Temperature,
pubmed-meshheading:11374890-Threonine
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pubmed:year |
2001
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pubmed:articleTitle |
Ray38p, a homolog of a purine motif triple-helical DNA-binding protein, Stm1p, is a ribosome-associated protein and dissociated from ribosomes prior to the induction of cycloheximide resistance in Candida maltosa.
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pubmed:affiliation |
Department of Biotechnology, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-8657, Japan.
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pubmed:publicationType |
Journal Article
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