Evidence for two protein factors in the transfer of amino acids from soluble-RNA to ribonucleoprotein particles

Fessenden, June M.; Moldave, Kivie

doi:10.1016/0006-291x(61)90136-x

Cited by 51 publications

(10 citation statements)

References 7 publications

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“…Scriba and Reddy (12) have found that the factor (s) responsible for the increased transfer activity of the soluble cell fraction after prolonged ACTH administration possesses characteristics which suggest identification as the transfer enzymes (13)(14)(15). They also observed that the pig adrenal assay system is particularly well suited to reflect changes in the amount or activity of transfer factor present in the soluble cell fraction.…”

Section: -Hour Experimentsmentioning

confidence: 93%

Early Effects of ACTH on Adrenal Protein Synthesis

Farese

1966

Endocrinology

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The sequential changes in activity of adrenal subcellular fractions for supporting incorporation of 14 C-amino acid into protein in a cell-free system have been followed during the first 24 hr of in vivo ACTH administration. During the first 2-4 hr of ACTH stimulation the incorporating activity of the 15,000 Xg supernatant is decreased, and this appears to be due to a decrease in microsomal activity. The decrease in microsomal activity is accompanied by a parallel decrease in microsomal (ribosomal) RNA, suggesting that ACTH, in the doses employed, results in an early enhancement of microsomal RNA turnover. In contrast to the early decrease in microsomal activity, there is concomitantly a moderate, transient increase in soluble cell fraction activity which appears to be due to an increase in soluble transfer enzymes. Subsequent to these changes at 2-4 hr, microsomal activity and microsomal RNA increase progressively, while soluble cell fraction activity decreases transiently and then increases. The reciprocal nature of the changes in soluble cell fraction activity relative to the changes in microsomal activity and microsomal RNA may possibly reflect the existence of distribution equilibrium of the transfer enzymes between soluble cell fraction and operative ribosomal sites. Thus, some of the early changes in soluble cell fraction activity may be secondary to the ribosomal changes. Additionally, in view of the early gross inhibitory effects of ACTH on adrenal protein synthesis, it seems likely that, if the steroidogenic action of ACTH is mediated via protein synthesis, it would be via the synthesis of selected protein rather than total adrenal protein. (Endocrinology 78: 125, 1966) ADMINISTRATION of ACTH for one ±\. or more days enhances the activity of cell-free extracts of the rat adrenal for incorporating amino acid into protein (1, 2). This effect of ACTH has been found to be due to increases in the activities of both soluble cell fraction (1) and microsomes (2). While the sequential changes in the amino acid-incorporating activities of these subcellular fractions have been well studied during relatively prolonged ACTH administration (1 through 12 days) (3), considerably less information is available on the early effects of ACTH on these

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Section: -Hour Experimentsmentioning

confidence: 93%

Early Effects of ACTH on Adrenal Protein Synthesis

Farese

1966

Endocrinology

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“…The incorporation of lysine with poly A is stimulated in a similar fashion by fractions A and B (lines 4, 5, and 6). Fessenden and Moldave (1961), working with a rat liver system, and Bishop and Schweet (1961), working with a reticulocyte system, have also independently reported the separation of the transfer enzymes into two fractions. The association of a ribosome requiring GTPase activity with the transfer enzymes was first observed by Dr. Monro in our laboratory .…”

Section: Preliminary Characterization Of the Two Fractions Essential mentioning

confidence: 94%

Formation of Peptide Bonds--I: Peptide Formation from Aminoacyl-S-RNA

Nakamoto¹,

Conway²,

Allende³

et al. 1963

Cold Spring Harbor Symposia on Quantitative Biology

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“…Although full aminoacyl-tRNA synthetase activity required the addition ofexcess of tRNA, the complete protein-synthesizing system was fully active in the presence of its own intrinsic tRNA. This is presumably due to the cyclical usage of tRNA in the cytoplasm (Nathans & Lipmann, 1961;Fessenden & Moldave, 1961;Noll et al, 1963).…”

Section: Animalmentioning

confidence: 99%

“…Aminoacyl-tRNA synthetase activity catalyses the activation of amino acids and the aminoacylation of tRNA, and the aminoacyl-tRNA transferase enzymes transfer the aminoacyl group from aminoacyl-tRNA to nascent protein at the ribosomal site (Fessenden & Moldave, 1961). The present method for the assay of cytoplasmic aminoacyl-tRNA synthetase activity measures the rate of incorporation of 'IC-labelled amino acid into aminoacyl-tRNA in the presence of an excess of tRNA.…”

mentioning

confidence: 99%

Myocardial aminoacyl-transfer-ribonucleic acid synthetase and aminoacyl-transferring enzyme activity

Gibson

Harris

1972

Biochemical Journal

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The properties of cytoplasmic aminoacyl-tRNA synthetase and aminoacyl-transferring enzymes in the myocardium were examined and methods for the assay of the activity of these enzyme systems were developed. Aminoacyl-tRNA synthetase activity was measured from the rate of incorporation of (14)C-labelled amino acid into aminoacyl-tRNA. Transferase activity was measured from the rate of incorporation of amino[(14)C]acyl-tRNA into protein in the presence of a standard preparation of hepatic ribosomes. Aminoacyl-tRNA synthetase activity is labile once the heart has been homogenized, whereas transferase activity is stable. The source of energy for synthetase activity is ATP; that for transferase is GTP. Transferase activity was inhibited by puromycin and stimulated by dithiothreitol, whereas synthetase activity was unaffected.

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Evidence for two protein factors in the transfer of amino acids from soluble-RNA to ribonucleoprotein particles

Cited by 51 publications

References 7 publications

Early Effects of ACTH on Adrenal Protein Synthesis

Early Effects of ACTH on Adrenal Protein Synthesis

Formation of Peptide Bonds--I: Peptide Formation from Aminoacyl-S-RNA

Myocardial aminoacyl-transfer-ribonucleic acid synthetase and aminoacyl-transferring enzyme activity

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