Published in

De Gruyter, Biological Chemistry, 11(400), p. 1397-1427, 2019

DOI: 10.1515/hsz-2019-0182

Links

Tools

Export citation

Search in Google Scholar

Exceptionally versatile – arginine in bacterial post-translational protein modifications

Journal article published in 2019 by Jürgen Lassak ORCID, Franziska Koller ORCID, Ralph Krafczyk ORCID, Wolfram Volkwein
Distributing this paper is prohibited by the publisher
Distributing this paper is prohibited by the publisher

Full text: Unavailable

Red circle
Preprint: archiving forbidden
Red circle
Postprint: archiving forbidden
Orange circle
Published version: archiving restricted
Data provided by SHERPA/RoMEO

Abstract

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.