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Arginyltransferase: A Personal and Historical Perspective

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Protein Arginylation

Part of the book series: Methods in Molecular Biology ((MIMB,volume 1337))

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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

  1. Soffer RL, Mendelsohn N (1966) Incorporation of arginine by a soluble system from sheep thyroid. Biochem Biophys Res Commun 23:252–258

    Article  CAS  PubMed  Google Scholar 

  2. Kaji H, Novelli GD, Kaji A (1963) A soluble amino acid-incorporating system from rat liver. Biochim Biophys Acta 76:474–477

    Article  CAS  PubMed  Google Scholar 

  3. 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

    CAS  PubMed  Google Scholar 

  4. Soffer RL (1968) The arginine transfer reaction. Biochim Biophys Acta 155:228–240

    Article  CAS  PubMed  Google Scholar 

  5. 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

    Article  CAS  PubMed  Google Scholar 

  6. 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

    CAS  PubMed  Google Scholar 

  7. Soffer RL (1971) Enzymatic modification of proteins IV. Arginylation of bovine thyroglobulin. J Biol Chem 246:1481–1484

    CAS  PubMed  Google Scholar 

  8. Soffer RL (1971) Enzymatic modification of proteins V. Protein acceptor specificity in the arginine-transfer reaction. J Biol Chem 246:1602–1606

    CAS  PubMed  Google Scholar 

  9. Soffer RL, Capra JD (1971) Enzymatic probe for accessibility of NH2-terminal residues in immunoglobulins. Nat New Biol 233:44–45

    Article  CAS  PubMed  Google Scholar 

  10. Soffer RL (1973) Peptide acceptors in the arginine transfer reaction. J Biol Chem 248:2918–2921

    CAS  PubMed  Google Scholar 

  11. 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

    CAS  PubMed  Google Scholar 

  12. Soffer RL (1973) Peptide acceptors in the leucine, phenylalanine transfer reaction. J Biol Chem 248:8424–8428

    CAS  PubMed  Google Scholar 

  13. Soffer RL, Deutch CE (1975) Arginyl-tRNA-protein transferase in eukaryotic protists. Biochem Biophys Res Commun 64:926–931

    Article  CAS  PubMed  Google Scholar 

  14. Savage M, Soffer RL, Leibowitz MJ (1983) A mutant of Saccharomyces cerevisiae defective in arginyl-tRNA-protein transferase. Curr Genet 7:285–288

    Article  CAS  PubMed  Google Scholar 

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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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Correspondence to Richard L. Soffer .

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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

  • Print ISBN: 978-1-4939-2934-4

  • Online ISBN: 978-1-4939-2935-1

  • eBook Packages: Springer Protocols

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