Exploring the diversity of protein modifications: Special bacterial phosphorylation systems

Research output: Contribution to journalArticleResearchpeer review

Authors

  • Ivan Mijakovic
  • Christophe Grangeasse
  • Kürşad Turgay

Research Organisations

External Research Organisations

  • Chalmers University of Technology
  • Technical University of Denmark
  • Université Claude Bernard Lyon 1
View graph of relations

Details

Original languageEnglish
Pages (from-to)398-417
Number of pages20
JournalFEMS microbiology reviews
Volume40
Issue number3
Publication statusPublished - May 2016

Abstract

Protein modifications not only affect protein homeostasis but can also establish new cellular protein functions and are important components of complex cellular signal sensing and transduction networks. Among these post-translational modifications, protein phosphorylation represents the one that has been most thoroughly investigated. Unlike in eukarya, a large diversity of enzyme families has been shown to phosphorylate and dephosphorylate proteins on various amino acids with different chemical properties in bacteria. In this review, after a brief overview of the known bacterial phosphorylation systems, we focus on more recently discovered and less widely known kinases and phosphatases. Namely, we describe in detail tyrosine- and arginine-phosphorylation together with some examples of unusual serine-phosphorylation systems and discuss their potential role and function in bacterial physiology, and regulatory networks. Investigating these unusual bacterial kinase and phosphatases is not only important to understand their role in bacterial physiology but will help to generally understand the full potential and evolution of protein phosphorylation for signal transduction, protein modification and homeostasis in all cellular life.

Keywords

    Protein arginine phosphorylation, Protein homeostasis, Protein kinase/phosphatase, Protein modification, Protein serine/threonine phosphorylation, Protein-tyrosine phosphorylation

ASJC Scopus subject areas

Sustainable Development Goals

Cite this

Exploring the diversity of protein modifications: Special bacterial phosphorylation systems. / Mijakovic, Ivan; Grangeasse, Christophe; Turgay, Kürşad.
In: FEMS microbiology reviews, Vol. 40, No. 3, 05.2016, p. 398-417.

Research output: Contribution to journalArticleResearchpeer review

Mijakovic I, Grangeasse C, Turgay K. Exploring the diversity of protein modifications: Special bacterial phosphorylation systems. FEMS microbiology reviews. 2016 May;40(3):398-417. doi: 10.1093/femsre/fuw003
Mijakovic, Ivan ; Grangeasse, Christophe ; Turgay, Kürşad. / Exploring the diversity of protein modifications : Special bacterial phosphorylation systems. In: FEMS microbiology reviews. 2016 ; Vol. 40, No. 3. pp. 398-417.
Download
@article{b58ee567e278491b83b5150d80ee6d91,
title = "Exploring the diversity of protein modifications: Special bacterial phosphorylation systems",
abstract = "Protein modifications not only affect protein homeostasis but can also establish new cellular protein functions and are important components of complex cellular signal sensing and transduction networks. Among these post-translational modifications, protein phosphorylation represents the one that has been most thoroughly investigated. Unlike in eukarya, a large diversity of enzyme families has been shown to phosphorylate and dephosphorylate proteins on various amino acids with different chemical properties in bacteria. In this review, after a brief overview of the known bacterial phosphorylation systems, we focus on more recently discovered and less widely known kinases and phosphatases. Namely, we describe in detail tyrosine- and arginine-phosphorylation together with some examples of unusual serine-phosphorylation systems and discuss their potential role and function in bacterial physiology, and regulatory networks. Investigating these unusual bacterial kinase and phosphatases is not only important to understand their role in bacterial physiology but will help to generally understand the full potential and evolution of protein phosphorylation for signal transduction, protein modification and homeostasis in all cellular life.",
keywords = "Protein arginine phosphorylation, Protein homeostasis, Protein kinase/phosphatase, Protein modification, Protein serine/threonine phosphorylation, Protein-tyrosine phosphorylation",
author = "Ivan Mijakovic and Christophe Grangeasse and K{\"u}r{\c s}ad Turgay",
note = "Publisher Copyright: {\textcopyright} FEMS 2016. Copyright: Copyright 2017 Elsevier B.V., All rights reserved.",
year = "2016",
month = may,
doi = "10.1093/femsre/fuw003",
language = "English",
volume = "40",
pages = "398--417",
journal = "FEMS microbiology reviews",
issn = "0168-6445",
publisher = "Oxford University Press",
number = "3",

}

Download

TY - JOUR

T1 - Exploring the diversity of protein modifications

T2 - Special bacterial phosphorylation systems

AU - Mijakovic, Ivan

AU - Grangeasse, Christophe

AU - Turgay, Kürşad

N1 - Publisher Copyright: © FEMS 2016. Copyright: Copyright 2017 Elsevier B.V., All rights reserved.

PY - 2016/5

Y1 - 2016/5

N2 - Protein modifications not only affect protein homeostasis but can also establish new cellular protein functions and are important components of complex cellular signal sensing and transduction networks. Among these post-translational modifications, protein phosphorylation represents the one that has been most thoroughly investigated. Unlike in eukarya, a large diversity of enzyme families has been shown to phosphorylate and dephosphorylate proteins on various amino acids with different chemical properties in bacteria. In this review, after a brief overview of the known bacterial phosphorylation systems, we focus on more recently discovered and less widely known kinases and phosphatases. Namely, we describe in detail tyrosine- and arginine-phosphorylation together with some examples of unusual serine-phosphorylation systems and discuss their potential role and function in bacterial physiology, and regulatory networks. Investigating these unusual bacterial kinase and phosphatases is not only important to understand their role in bacterial physiology but will help to generally understand the full potential and evolution of protein phosphorylation for signal transduction, protein modification and homeostasis in all cellular life.

AB - Protein modifications not only affect protein homeostasis but can also establish new cellular protein functions and are important components of complex cellular signal sensing and transduction networks. Among these post-translational modifications, protein phosphorylation represents the one that has been most thoroughly investigated. Unlike in eukarya, a large diversity of enzyme families has been shown to phosphorylate and dephosphorylate proteins on various amino acids with different chemical properties in bacteria. In this review, after a brief overview of the known bacterial phosphorylation systems, we focus on more recently discovered and less widely known kinases and phosphatases. Namely, we describe in detail tyrosine- and arginine-phosphorylation together with some examples of unusual serine-phosphorylation systems and discuss their potential role and function in bacterial physiology, and regulatory networks. Investigating these unusual bacterial kinase and phosphatases is not only important to understand their role in bacterial physiology but will help to generally understand the full potential and evolution of protein phosphorylation for signal transduction, protein modification and homeostasis in all cellular life.

KW - Protein arginine phosphorylation

KW - Protein homeostasis

KW - Protein kinase/phosphatase

KW - Protein modification

KW - Protein serine/threonine phosphorylation

KW - Protein-tyrosine phosphorylation

UR - http://www.scopus.com/inward/record.url?scp=84975775571&partnerID=8YFLogxK

U2 - 10.1093/femsre/fuw003

DO - 10.1093/femsre/fuw003

M3 - Article

C2 - 26926353

AN - SCOPUS:84975775571

VL - 40

SP - 398

EP - 417

JO - FEMS microbiology reviews

JF - FEMS microbiology reviews

SN - 0168-6445

IS - 3

ER -