Advertisement

Nα-Acetylation of Eukaryotic Proteins: Purification and Characterization of Yeast Nα-Acetyltransferase and Acetylcoenzyme A Hydrolase

  • Fang-Jen S. Lee
  • Lee-Wen Lin
  • John A. Smith

Abstract

Nα-acetylation is the most common N-terminal modification of eukaryotic proteins, but its physiological significance is still an enigma. Many proteins are known to be Nα-acetylated (Tsunasawa and Sakiyama 1984; Driessen et al 1985). For example, > 80% of the intracellular, soluble proteins in mouse L-cells and Ehrlich ascites cells are Nα-acetylated (Brown and Roberts 1976; Brown 1979). Although the biological role of Nα-acetylation in protein degradation and protein secretion has been investigated, much is still unknown.

Keywords

Eukaryotic Protein Protein Sequence Analysis Catabolize Amino Acid Ehrlich Ascites Cell Yeast Alcohol Dehydrogenase 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Brown JL (1979) A comparison of the turnover of α-N-acetylated and nonacetylated mouse L-cell proteins. J Biol Chem 254: 1447–1449PubMedGoogle Scholar
  2. Brown JL, Roberts WK (1976) Evidence that approximately eighty per cent of the soluble proteins from Ehrlich ascites cells are Na-acetylated. J Biol Chem 251: 1009–1014PubMedGoogle Scholar
  3. Chin CCQ, Brewer JM, Wold F (1981) The amino acid sequence of yeast enolase. J Biol Chem 256: 1377–1384PubMedGoogle Scholar
  4. Driessen HPC, De Jong WW, Tesser GI, Bloemendal H (1985) The mechanism of N-terminal acetylation of proteins. CRC Crit Rev Biochem 18: 281–325PubMedCrossRefGoogle Scholar
  5. Kobayashi K, Smith JA (1987) Acyl-peptide hydrolase from rat liver: characterization of enzyme reaction. J Biol Chem 262: 11435–11445PubMedGoogle Scholar
  6. Lee F-JS, Lin L-W, Smith JA (1988) Purification and characterization of Nα-acetyltransferase from Saccharomyces cerevisiae. J Biol Chem 263:in pressGoogle Scholar
  7. Persson B, C. Flinta C, von Heijne G, Jornvall H (1985) Structures of N-terminally acetylated proteins. Eur J Biochem 152: 523–527PubMedCrossRefGoogle Scholar
  8. Radhakrishna G, Wold F (1986) Rabbit muscle extracts catalyze the specific removal of N-acetylmethionine from acetylated peptides. J Biol Chem 261: 9572–9575PubMedGoogle Scholar
  9. Smith JA, Kobayashi K, Yeadon JE (1988) Nα-Acetylation of proteins and removal of acetylated amino acids. In: Marshak DR, Liu DT (Eds) Therapeutic peptides and proteins: assessing the new technologies, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY, pp 69–78Google Scholar
  10. Tsunasawa S, Sakiyama F (1984) Amino-terminal acetylation of proteins: An overview. Methods Enzymol 106: 165–170PubMedCrossRefGoogle Scholar
  11. Tsunasawa S, Narita K, Ogata K (1975) Purification and properties of acylamino acid-releasing enzyme from rat liver. J Biochem (Tokyo) 77: 89–102Google Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 1989

Authors and Affiliations

  • Fang-Jen S. Lee
    • 1
    • 2
  • Lee-Wen Lin
    • 1
    • 2
  • John A. Smith
    • 1
    • 3
    • 4
  1. 1.Department of Molecular BiologyMassachusetts General HospitalBostonUSA
  2. 2.Department of GeneticsHarvard Medical SchoolBostonUSA
  3. 3.Department of PathologyMassachusetts General HospitalBostonUSA
  4. 4.Department of PathologyHarvard Medical SchoolBostonUSA

Personalised recommendations