Exceptionally versatile - arginine in bacterial post-translational protein modifications

Biol Chem. 2019 Oct 25;400(11):1397-1427. doi: 10.1515/hsz-2019-0182.

Abstract

Post-translational modifications (PTM) are the evolutionary solution to challenge and extend the boundaries of genetically predetermined proteomic diversity. As PTMs are highly dynamic, they also hold an enormous regulatory potential. It is therefore not surprising that out of the 20 proteinogenic amino acids, 15 can be post-translationally modified. Even the relatively inert guanidino group of arginine is subject to a multitude of mostly enzyme mediated chemical changes. The resulting alterations can have a major influence on protein function. In this review, we will discuss how bacteria control their cellular processes and develop pathogenicity based on post-translational protein-arginine modifications.

Keywords: advanced glycation end products; arginine ADP-ribosylation; arginine acetylation; arginine glycosylation; arginine hydroxylation; arginine methylation; arginine phosphorylation.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Arginine / metabolism*
  • Bacterial Proteins / metabolism*
  • Protein Processing, Post-Translational*
  • Proteomics

Substances

  • Bacterial Proteins
  • Arginine