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Post-Translational Modifications in Corynebacterium glutamicum

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Corynebacterium glutamicum

Part of the book series: Microbiology Monographs ((MICROMONO,volume 23))

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Abstract

Newly synthesized proteins are subject to several post-translational modifications (PTMs). These PTMs can create diverse proteins from a single gene and are important for the function of certain proteins in a given situation. Recent advances in mass spectrometry (MS)-based proteomics have enabled the global detection of PTMs of bacterial proteins. In Corynebacterium and other actinobacteria, common PTMs (e.g., phosphorylation and acetylation) as well as uncommon PTMs (e.g., pupylation, mycoloylation, and mycothiolation) have been detected. In this chapter, the features of six representative PTMs found in Corynebacterium glutamicum, phosphorylation, acylation, pupylation, mycoloylation, mycothiolation, and glycosylation, and their roles in protein regulation are described.

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  1. Biotechnology Research Center, The University of Tokyo, Tokyo, Japan

    Saori Kosono

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  1. Molecular Microbiology and Biotechnology, Research Institute of Innovative Technology, Kyoto, Japan

    Masayuki Inui

  2. Molecular Microbiology and Biotechnology, Research Institute of Innovative Technology, Kyoto, Japan

    Koichi Toyoda

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Kosono, S. (2020). Post-Translational Modifications in Corynebacterium glutamicum . In: Inui, M., Toyoda, K. (eds) Corynebacterium glutamicum. Microbiology Monographs, vol 23. Springer, Cham. https://doi.org/10.1007/978-3-030-39267-3_6

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