Posttranslational NH2-Terminal Aminoacylation

C. E. Deutch, R. C. Scarpulla, R. L. Soffer

Research output: Contribution to journalArticlepeer-review

9 Scopus citations

Abstract

This chapter presents an overview of posttranslational NH2-terminal aminoacylation. Aminoacyl-tRNA protein transferases catalyze the addition of certain amino acids to the NH2-terminus of specific proteins and peptides. These enzymes constitute one mechanism for the posttranslational modification of NH2-termini and may contribute to the heterogeneity in NH2-terminal residues, which has been observed in bulk proteins of both prokaryotes and eukaryotes. Modifications of the NH2-terminus can be classified into three basic types: (1) cleavage reactions, in which a formyl, methionyl, or other residue is removed; (2) alteration reactions, in which it is converted to another type of molecule, such as an α-keto acid or a cyclized derivative; and (3) addition reactions, including acetylation, phosphorylation, and aminoacylation, in which small molecules are added to it. The chapter focuses on the biochemistry and physiological function of the reactions catalyzed by aminoacyl-tRNA protein transferases.

Original languageEnglish (US)
Pages (from-to)1-28
Number of pages28
JournalCurrent topics in cellular regulation
Volume13
Issue numberC
DOIs
StatePublished - Jan 1 1978

ASJC Scopus subject areas

  • Cell Biology

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