Abstract
Three proteins required for poly(U)-directed polyphenylalanine synthesis have been separated from yeast. Two of the factors correspond to the elongation factors 1 and 2 described for other eukaryotic systems, according to the criteria of phenylalanyl-tRNA binding and diphtheria toxin-catalyzed ADP-ribosylation. The third protein, while absolutely required for polyphenylalanine synthesis, was a more active ribosome-dependent GTPase than elongation factor 2.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Adenosine Diphosphate / metabolism
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Cell-Free System
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Diphtheria Toxin / metabolism
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Fusidic Acid / pharmacology
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GTP Phosphohydrolase-Linked Elongation Factors / antagonists & inhibitors
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GTP Phosphohydrolase-Linked Elongation Factors / metabolism*
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Peptide Chain Elongation, Translational*
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Peptide Elongation Factors / isolation & purification*
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Phenylalanine / metabolism
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Phosphoric Monoester Hydrolases / metabolism*
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Poly U / metabolism
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RNA, Transfer / metabolism
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Ribosomes / metabolism*
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Saccharomyces cerevisiae / enzymology*
Substances
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Diphtheria Toxin
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Peptide Elongation Factors
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Poly U
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Phenylalanine
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Fusidic Acid
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Adenosine Diphosphate
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RNA, Transfer
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Phosphoric Monoester Hydrolases
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GTP Phosphohydrolase-Linked Elongation Factors