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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
15
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pubmed:dateCreated |
1985-8-28
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pubmed:abstractText |
The activity of bovine mitochondrial ribosomes with elongation factors from a variety of sources including the mitochondria of lower eukaryotes, chloroplasts, Gram-negative bacteria, Gram-positive bacteria, and the eukaryotic cell cytoplasm has been investigated. Bovine mitochondrial ribosomes are active with homologous mitochondrial elongation factor (EF)-G but display no activity with the mitochondrial or chloroplast translocases from the lower eukaryote Euglena gracilis, with Escherichia coli or Bacillus subtilis EF-G or with cytoplasmic EF-2. In contrast to the results obtained with the translocases, E. coli EF-Tu, B. subtilis EF-Tu, and Euglena chloroplast EF-Tu all function to a significant extent on the mitochondrial ribosomes. Cytoplasmic EF-1 has barely detectable activity on the animal mitochondrial ribosomes. The polymerization of phenylalanine by these ribosomes is dependent on poly(U), displays a rather broad Mg2+ optimum around 12 mM, and proceeds most rapidly at low monovalent ion concentrations.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Magnesium,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Elongation Factor G,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Elongation Factor Tu,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Elongation Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Phenylalanine
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
260
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
8721-5
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:4040515-Animals,
pubmed-meshheading:4040515-Cattle,
pubmed-meshheading:4040515-Magnesium,
pubmed-meshheading:4040515-Mitochondria,
pubmed-meshheading:4040515-Peptide Elongation Factor G,
pubmed-meshheading:4040515-Peptide Elongation Factor Tu,
pubmed-meshheading:4040515-Peptide Elongation Factors,
pubmed-meshheading:4040515-Phenylalanine,
pubmed-meshheading:4040515-Protein Biosynthesis,
pubmed-meshheading:4040515-Ribosomes
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pubmed:year |
1985
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pubmed:articleTitle |
Bovine mitochondrial ribosomes. Elongation factor specificity.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, U.S. Gov't, P.H.S.
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