Exceptionally versatile – arginine in bacterial post-translational protein modifications-Reference-Cited by-同舟云学术

Exceptionally versatile – arginine in bacterial post-translational protein modifications

Published:2019-07-09 Issue:11 Volume:400 Page:1397-1427
ISSN:1437-4315
Container-title:Biological Chemistry
language:en
Short-container-title:

Author:

Lassak Jürgen¹^ORCID,Koller Franziska¹^ORCID,Krafczyk Ralph¹^ORCID,Volkwein Wolfram¹

Affiliation:

1. Center for Integrated Protein Science Munich (CiPSM), Department of Biology I, Microbiology , Ludwig-Maximilians-Universität München , Grosshaderner Strasse 2-4 , D-82152 Planegg , Germany

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.

Funder

Deutsche Forschungsgemeinschaft

Publisher

Walter de Gruyter GmbH

Subject

Clinical Biochemistry,Molecular Biology,Biochemistry

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