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pArg_deg_signal SIGNED

No stress with pArg: Mechanisms of a distinct phospho-mark to coordinate stress response and protein quality control

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EC-Contrib. €

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Partnership

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 pArg_deg_signal project word cloud

Explore the words cloud of the pArg_deg_signal project. It provides you a very rough idea of what is the project "pArg_deg_signal" about.

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Project "pArg_deg_signal" data sheet

The following table provides information about the project.

Coordinator
FORSCHUNGSINSTITUT FUR MOLEKULARE PATHOLOGIE GESELLSCHAFT MBH 

Organization address
address: CAMPUS-VIENNA-BIOCENTER 1
city: WIEN
postcode: 1030
website: www.imp.ac.at

contact info
title: n.a.
name: n.a.
surname: n.a.
function: n.a.
email: n.a.
telephone: n.a.
fax: n.a.

 Coordinator Country Austria [AT]
 Project website https://www.imp.ac.at/groups/tim-clausen/
 Total cost 2˙499˙299 €
 EC max contribution 2˙499˙299 € (100%)
 Programme 1. H2020-EU.1.1. (EXCELLENT SCIENCE - European Research Council (ERC))
 Code Call ERC-2015-AdG
 Funding Scheme ERC-ADG
 Starting year 2016
 Duration (year-month-day) from 2016-10-01   to  2021-09-30

 Partnership

Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    FORSCHUNGSINSTITUT FUR MOLEKULARE PATHOLOGIE GESELLSCHAFT MBH AT (WIEN) coordinator 2˙499˙299.00

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 Project objective

Cellular proteins are prone to misfolding and aggregation, particularly under harsh environmental conditions. To counteract this danger, all organisms from bacteria to humans evolved sophisticated protein quality control networks. The mechanisms employed in them tend to represent some of the most exciting biochemistry occurring in living cells.

In Gram-positive bacteria, the key factors combating protein damage include a specialized protein kinase phosphorylating arginine residues (McsB), the central housekeeping protease (ClpP), as well as a AAA chaperone targeting aggregated proteins (ClpC). We find this quality-control system, organized around a distinct protein phospho mark (phosphoarginine, pArg), a fascinating model to investigate novel principles of dealing with proteotoxic stress.

Using an integrative approach, we will delineate the precise role of protein arginine phosphorylation in the bacterial stress response. We will first analyze how this unique modification influences the stability and function of targeted proteins in vitro and in vivo. We are particularly interested in the possibility of pArg serving as a bacterial, ubiquitin-like degradation signal. We will then address the mechanism and regulation of the protein arginine kinase McsB. This analysis will uncover the specificity of the pArg tagging system. Additionally, these studies will reveal enzymatic innovations connected with the pArg chemistry that, due to the dependence of bacterial virulence on McsB, are of pharmaceutical interest. To address the further processing of pArg-modified proteins, we will perform an in-depth structural characterization of ClpC and related AAA disaggregases. A better understanding of the mechanism and regulation of these HSP100 molecular machines is also highly relevant to uncover general principles of how cells deal with toxic protein aggregates and, in parallel, keep control over their potentially dangerous shredding devices.

 Publications

year authors and title journal last update
List of publications.
2019 Marcin J. Suskiewicz, Bence Hajdusits, Rebecca Beveridge, Alexander Heuck, Lam Dai Vu, Robert Kurzbauer, Katja Hauer, Vanessa Thoeny, Klaus Rumpel, Karl Mechtler, Anton Meinhart, Tim Clausen
Structure of McsB, a protein kinase for regulated arginine phosphorylation
published pages: 510-518, ISSN: 1552-4450, DOI: 10.1038/s41589-019-0265-y
Nature Chemical Biology 15/5 2019-09-02
2019 Marcin J. Suskiewicz, Bence Hajdusits, Rebecca Beveridge, Alexander Heuck, Lam Dai Vu, Robert Kurzbauer, Katja Hauer, Vanessa Thoeny, Klaus Rumpel, Karl Mechtler, Anton Meinhart, Tim Clausen
Structure of McsB, a protein kinase for regulated arginine phosphorylation
published pages: 510-518, ISSN: 1552-4450, DOI: 10.1038/s41589-019-0265-y
Nature Chemical Biology 15/5 2019-07-22
2016 Alexander Heuck, Sonja Schitter-Sollner, Marcin Józef Suskiewicz, Robert Kurzbauer, Juliane Kley, Alexander Schleiffer, Pascaline Rombaut, Franz Herzog, Tim Clausen
Structural basis for the disaggregase activity and regulation of Hsp104
published pages: , ISSN: 2050-084X, DOI: 10.7554/eLife.21516
eLife 5 2019-06-13

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