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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1990-9-10
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pubmed:abstractText |
The functional role of the deazaguanine-derivative queuine was investigated using virus-transformed erythroleukaemic cells of mice as a model. The two-dimensional patterns of [35S]methionine-labelled proteins on two-dimensional O'Farrell gels of queuine-deficient (Q-), compared with queuine-supplemented (Q+) growing cells, showed specific characteristic alterations in the synthesis of 36 and 42 kd basic proteins. According to pI values and immunoreactivity with anti-LDH antibodies, the 36 kd proteins represent various forms of LDH A subunits or closely related proteins. Cell-free systems of protein synthesis were established from growing (Q-) or (Q+) cells. Addition of 3 x 10(-8) M queuine to the (Q-) in vitro system inhibited the incorporation of [35S]methionine into total protein to approximately 20%; raising the concentration of queuine up to 1 x 10(-6) M did not increase the inhibitory effect appreciably. In the (Q-) system, a series of 36 kd proteins, with pI values corresponding to LDH A isoforms, were synthesized. The in vitro synthesis of these proteins was completely inhibited by addition of queuine at a concentration of 3 x 10(-8) M. Furthermore, the expression of certain other proteins was lower in the (Q+) than in the (Q-) in vitro system. Labelling of growing (Q+) or (Q-) cells with [32P]orthophosphate and subsequent analysis of phosphoproteins on two-dimensional O'Farrell gels showed that queuine inhibited the synthesis of distinct phosphoproteins. Protein synthesis performed in cell-free (Q-) or (Q+) systems in the presence of non-labelled amino acids and 32P-labelled gamma ATP also indicated that queuine interferes with the synthesis and/or phosphorylation of particular phosphoproteins.
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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/Guanine,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/L-Lactate Dehydrogenase,
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/queuine
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0951-6433
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
2
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
185-92
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:2378671-Animals,
pubmed-meshheading:2378671-Cell-Free System,
pubmed-meshheading:2378671-Friend murine leukemia virus,
pubmed-meshheading:2378671-Guanine,
pubmed-meshheading:2378671-Isoenzymes,
pubmed-meshheading:2378671-L-Lactate Dehydrogenase,
pubmed-meshheading:2378671-Leukemia, Erythroblastic, Acute,
pubmed-meshheading:2378671-Mice,
pubmed-meshheading:2378671-Neoplasm Proteins,
pubmed-meshheading:2378671-Phosphoproteins,
pubmed-meshheading:2378671-Phosphorylation,
pubmed-meshheading:2378671-Protein Biosynthesis,
pubmed-meshheading:2378671-Protein Processing, Post-Translational,
pubmed-meshheading:2378671-Tumor Cells, Cultured
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pubmed:year |
1990
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pubmed:articleTitle |
Possible involvement of queuine in control mechanisms of protein synthesis and protein phosphorylation in eukaryotes.
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pubmed:affiliation |
Institut für Biochemie, Universität Erlangen-Nürnberg, FRG.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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