Abstract
In the late 1960s and early 1970s, characterization of arginylation has been spearheaded via biochemical studies that enabled the first characterization of ATE1 and its substrate specificity. This essay summarized the recollections and insights from the era of research that followed from the original discovery of arginylation and led up to the identification of the arginylation enzyme.
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References
Soffer RL, Mendelsohn N (1966) Incorporation of arginine by a soluble system from sheep thyroid. Biochem Biophys Res Commun 23:252–258
Kaji H, Novelli GD, Kaji A (1963) A soluble amino acid-incorporating system from rat liver. Biochim Biophys Acta 76:474–477
Weinstein IB, Osserman EF (1964) Amino acid incorporation by a cell free system from plasma cell tumors. Acta Unio Int Contra Cancrum 20:932–936
Soffer RL (1968) The arginine transfer reaction. Biochim Biophys Acta 155:228–240
Soffer RL, Horinishi H (1969) Enzymatic modification of proteins I. General characteristics of the arginine-transfer reaction in rabbit liver cytoplasm. J Mol Biol 43:163–175
Soffer RL (1970) Enzymatic modification of proteins II. Purification and properties of the arginyl transfer ribonucleic acid-protein transferase from rabbit liver cytoplasm. J Biol Chem 245:731–737
Soffer RL (1971) Enzymatic modification of proteins IV. Arginylation of bovine thyroglobulin. J Biol Chem 246:1481–1484
Soffer RL (1971) Enzymatic modification of proteins V. Protein acceptor specificity in the arginine-transfer reaction. J Biol Chem 246:1602–1606
Soffer RL, Capra JD (1971) Enzymatic probe for accessibility of NH2-terminal residues in immunoglobulins. Nat New Biol 233:44–45
Soffer RL (1973) Peptide acceptors in the arginine transfer reaction. J Biol Chem 248:2918–2921
Leibowitz MJ, Soffer RL (1971) Enzymatic modification of proteins VI. Site of acylation of bovine serum albumin in the leucine, phenylalanine-transfer reaction. J Biol Chem 246:4431–4438
Soffer RL (1973) Peptide acceptors in the leucine, phenylalanine transfer reaction. J Biol Chem 248:8424–8428
Soffer RL, Deutch CE (1975) Arginyl-tRNA-protein transferase in eukaryotic protists. Biochem Biophys Res Commun 64:926–931
Savage M, Soffer RL, Leibowitz MJ (1983) A mutant of Saccharomyces cerevisiae defective in arginyl-tRNA-protein transferase. Curr Genet 7:285–288
Acknowledgments
I was fortunate to have very able students and fellows who shared my interest in aminoacyl transferases. They were, in alphabetical order, Charles E. Deutch, Hiroo Horinishi, Michael J. Leibowitz, Margaret Savage, and Richard C. Scarpulla.
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Soffer, R.L. (2015). Arginyltransferase: A Personal and Historical Perspective. In: Kashina, A. (eds) Protein Arginylation. Methods in Molecular Biology, vol 1337. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-2935-1_3
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DOI: https://doi.org/10.1007/978-1-4939-2935-1_3
Publisher Name: Humana Press, New York, NY
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Online ISBN: 978-1-4939-2935-1
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