Exceptionally versatile – arginine in bacterial post-translational protein modifications

• Published in: Biological chemistry Vol. 400; no. 11; pp. 1397 - 1427
• Main Authors: Lassak, Jürgen, Koller, Franziska, Krafczyk, Ralph, Volkwein, Wolfram
• Format: Journal Article
• Language: English
• Published: Germany De Gruyter 26.11.2019; Walter de Gruyter GmbH
• Subjects: advanced glycation end products; Amino acids; Arginine; Arginine - metabolism; arginine acetylation; arginine ADP-ribosylation; arginine glycosylation; arginine hydroxylation; arginine methylation; arginine phosphorylation; Bacterial Proteins - metabolism; Organic chemistry; Pathogenicity; Pathogens; Post-translation; Protein Processing, Post-Translational; Proteins; Proteomics; Translation; arginine methylation; arginine glycosylation; arginine hydroxylation; arginine acetylation; arginine ADP-ribosylation; arginine phosphorylation; advanced glycation end products
• ISSN: 1431-6730; 1437-4315; 1437-4315
• DOI: 10.1515/hsz-2019-0182

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.