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Updated: Jan 23, 2026

Identification of Post-translational Modifications of Plant Protein Complexes
Published on: February 22, 2014
Exceptionally versatile - arginine in bacterial post-translational protein modifications
Jürgen Lassak1, Franziska Koller1, Ralph Krafczyk1
1Center for Integrated Protein Science Munich (CiPSM), Department of Biology I, Microbiology, Ludwig-Maximilians-Universität München, Grosshaderner Strasse 2-4, D-82152 Planegg, Germany.
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.
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