N-terminal methylation of proteins: Structure, function and specificity

Ann Stock, Steven Clarke, Catherine Clarke, Jeff Stock

Research output: Contribution to journalReview article

68 Scopus citations

Abstract

A common site for the posttranslational modification of proteins is at the N-terminal α-amino group. Here we consider the enzymatic addition of one or more methyl groups that has been found to occur in several proteins. Although the methylated proteins have different overall functions, they all appear to be involved in large macromolecular structures such as ribosomes, myofibrils, nucleosomes, pilins, or flagella. Structural features at the N-termini of these methylated proteins suggest that sequences in this region may serve as recognition sites for only a few different types of methylating enzymes. Thus, we propose that three enzymes could account for the N-methylated species so far identified in bacteria, the hypothetical MAK, QP, and pilin methyltransferases, and a single additional enzyme, the hypothetical PK methyltransferase, could account for all of the α-amino methylations observed in eukaryotic cells. Finally, we discuss criteria that could be used in conjuction with primary sequence data to predict proteins that might be subject to methylation at their amino termini.

Original languageEnglish (US)
Pages (from-to)8-14
Number of pages7
JournalFEBS Letters
Volume220
Issue number1
DOIs
StatePublished - Aug 10 1987

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Keywords

  • Methylalanine
  • Methylmethionine
  • Methylphenylalanine
  • Methylproline
  • N-terminus
  • Protein methylation

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