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Rat liver polysome N alpha-acetyltransferase: substrate specificity.

R Yamada1, R A Bradshaw

  • 1Department of Biological Chemistry, College of Medicine, University of California, Irvine 92717.

Biochemistry
|January 29, 1991
PubMed
Summary
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Rat liver N alpha-acetyltransferase (NAT) modifies peptides with specific N-terminal amino acids. Optimal substrate length is 10-11 residues, suggesting cotranslational acetylation of nascent protein chains.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • N-terminal acetylation is a common co-translational modification in eukaryotes.
  • Polysome-associated N alpha-acetyltransferase (NAT) is responsible for this process in rat liver.

Purpose of the Study:

  • To elucidate the substrate specificity of rat liver polysomal NAT.
  • To determine the optimal peptide length for NAT activity.

Main Methods:

  • Systematic modification of synthetic peptide sequences (S-Y-S-G-G-L-L-L) by substituting amino acids at N-terminal positions.
  • Assessment of peptide reactivity with rat liver NAT.
  • Evaluation of adrenocorticotropin (ACTH) peptides of varying lengths as substrates.

Main Results:

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  • N-terminal serine, alanine, methionine, leucine, and phenylalanine were permissive for modification.
  • Specific amino acids in the second and third positions significantly inhibited or blocked NAT activity.
  • Optimal substrate length was found to be 10-11 residues.
  • ACTH peptides were superior substrates compared to synthetic peptides of similar length.

Conclusions:

  • Rat liver NAT exhibits specific N-terminal amino acid preferences.
  • The enzyme functions optimally on nascent polypeptide chains of approximately 10-11 amino acids.
  • These findings support the role of polysome-catalyzed N alpha-acetylation as a co-translational event.