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Article ; Online: Structural basis of aggregate binding by the AAA+ disaggregase ClpG.

Katikaridis, Panagiotis / Simon, Bernd / Jenne, Timo / Moon, Seongjoon / Lee, Changhan / Hennig, Janosch / Mogk, Axel

2023 Volume 299, Issue 11, Page(s) 105336

Abstract: Severe heat stress causes massive loss of essential proteins by aggregation, necessitating a cellular activity that rescues aggregated proteins. This activity is executed by ATP-dependent, ring-forming, hexameric AAA+ disaggregases. Little is known about ...

Abstract	Severe heat stress causes massive loss of essential proteins by aggregation, necessitating a cellular activity that rescues aggregated proteins. This activity is executed by ATP-dependent, ring-forming, hexameric AAA+ disaggregases. Little is known about the recognition principles of stress-induced protein aggregates. How can disaggregases specifically target aggregated proteins, while avoiding binding to soluble non-native proteins? Here, we determined by NMR spectroscopy the core structure of the aggregate-targeting N1 domain of the bacterial AAA+ disaggregase ClpG, which confers extreme heat resistance to bacteria. N1 harbors a Zn
Language	English
Publishing date	2023-10-10
Publishing country	United States
Document type	Journal Article
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2023.105336
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Article: Resisting the Heat: Bacterial Disaggregases Rescue Cells From Devastating Protein Aggregation.

Katikaridis, Panagiotis / Bohl, Valentin / Mogk, Axel

Frontiers in molecular biosciences

2021 Volume 8, Page(s) 681439

Abstract: Bacteria as unicellular organisms are most directly exposed to changes in environmental growth conditions like temperature increase. Severe heat stress causes massive protein misfolding and aggregation resulting in loss of essential proteins. To ensure ... ...

Abstract	Bacteria as unicellular organisms are most directly exposed to changes in environmental growth conditions like temperature increase. Severe heat stress causes massive protein misfolding and aggregation resulting in loss of essential proteins. To ensure survival and rapid growth resume during recovery periods bacteria are equipped with cellular disaggregases, which solubilize and reactivate aggregated proteins. These disaggregases are members of the Hsp100/AAA+ protein family, utilizing the energy derived from ATP hydrolysis to extract misfolded proteins from aggregates via a threading activity. Here, we describe the two best characterized bacterial Hsp100/AAA+ disaggregases, ClpB and ClpG, and compare their mechanisms and regulatory modes. The widespread ClpB disaggregase requires cooperation with an Hsp70 partner chaperone, which targets ClpB to protein aggregates. Furthermore, Hsp70 activates ClpB by shifting positions of regulatory ClpB M-domains from a repressed to a derepressed state. ClpB activity remains tightly controlled during the disaggregation process and high ClpB activity states are likely restricted to initial substrate engagement. The recently identified ClpG (ClpK) disaggregase functions autonomously and its activity is primarily controlled by substrate interaction. ClpG provides enhanced heat resistance to selected bacteria including pathogens by acting as a more powerful disaggregase. This disaggregase expansion reflects an adaption of bacteria to extreme temperatures experienced during thermal based sterilization procedures applied in food industry and medicine. Genes encoding for ClpG are transmissible by horizontal transfer, allowing for rapid spreading of extreme bacterial heat resistance and posing a threat to modern food production.
Language	English
Publishing date	2021-05-04
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2814330-9
ISSN	2296-889X
ISSN	2296-889X
DOI	10.3389/fmolb.2021.681439
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Article ; Online: Basic mechanism of the autonomous ClpG disaggregase.

Katikaridis, Panagiotis / Römling, Ute / Mogk, Axel

The Journal of biological chemistry

2021 Volume 296, Page(s) 100460

Abstract: Bacterial survival during lethal heat stress relies on the cellular ability to reactivate aggregated proteins. This activity is typically executed by the canonical 70-kDa heat shock protein (Hsp70)-ClpB bichaperone disaggregase, which is most widespread ... ...

Abstract	Bacterial survival during lethal heat stress relies on the cellular ability to reactivate aggregated proteins. This activity is typically executed by the canonical 70-kDa heat shock protein (Hsp70)-ClpB bichaperone disaggregase, which is most widespread in bacteria. The ClpB disaggregase is a member of the ATPase associated with diverse cellular activities protein family and exhibits an ATP-driven threading activity. Substrate binding and stimulation of ATP hydrolysis depends on the Hsp70 partner, which initiates the disaggregation reaction. Recently elevated heat resistance in gamma-proteobacterial species was shown to be mediated by the ATPase associated with diverse cellular activities protein ClpG as an alternative disaggregase. Pseudomonas aeruginosa ClpG functions autonomously and does not cooperate with Hsp70 for substrate binding, enhanced ATPase activity, and disaggregation. With the underlying molecular basis largely unknown, the fundamental differences in ClpG- and ClpB-dependent disaggregation are reflected by the presence of sequence alterations and additional ClpG-specific domains. By analyzing the effects of mutants lacking ClpG-specific domains and harboring mutations in conserved motifs implicated in ATP hydrolysis and substrate threading, we show that the N-terminal, ClpG-specific N1 domain generally mediates protein aggregate binding as the molecular basis of autonomous disaggregation activity. Peptide substrate binding strongly stimulates ClpG ATPase activity by overriding repression by the N-terminal N1 and N2 domains. High ATPase activity requires two functional nucleotide binding domains and drives substrate threading which ultimately extracts polypeptides from the aggregate. ClpG ATPase and disaggregation activity is thereby directly controlled by substrate availability.
MeSH term(s)	Adenosine Triphosphatases/metabolism ; Adenosine Triphosphate/metabolism ; Antigens, Bacterial/metabolism ; Antigens, Bacterial/physiology ; Endopeptidase Clp/metabolism ; Endopeptidase Clp/physiology ; Escherichia coli/metabolism ; Escherichia coli Proteins/metabolism ; Escherichia coli Proteins/physiology ; HSP70 Heat-Shock Proteins/metabolism ; Heat-Shock Proteins/metabolism ; Heat-Shock Proteins/physiology ; Protein Aggregates ; Protein Binding ; Protein Domains/genetics
Chemical Substances	Antigens, Bacterial ; Escherichia coli Proteins ; HSP70 Heat-Shock Proteins ; Heat-Shock Proteins ; Protein Aggregates ; clpG protein, E coli (144998-09-4) ; Adenosine Triphosphate (8L70Q75FXE) ; Endopeptidase Clp (EC 3.4.21.92) ; Adenosine Triphosphatases (EC 3.6.1.-) ; ClpB protein, E coli (EC 3.6.1.3)
Language	English
Publishing date	2021-02-24
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2021.100460
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Article ; Online: The

Bohl, Valentin / Hollmann, Nele Merret / Melzer, Tobias / Katikaridis, Panagiotis / Meins, Lena / Simon, Bernd / Flemming, Dirk / Sinning, Irmgard / Hennig, Janosch / Mogk, Axel

eLife

2024 Volume 12

Abstract: Heat stress can cause cell death by triggering the aggregation of essential proteins. In bacteria, aggregated proteins are rescued by the canonical Hsp70/AAA+ (ClpB) bi-chaperone disaggregase. Man-made, severe stress conditions applied during, e.g., food ...

Abstract	Heat stress can cause cell death by triggering the aggregation of essential proteins. In bacteria, aggregated proteins are rescued by the canonical Hsp70/AAA+ (ClpB) bi-chaperone disaggregase. Man-made, severe stress conditions applied during, e.g., food processing represent a novel threat for bacteria by exceeding the capacity of the Hsp70/ClpB system. Here, we report on the potent autonomous AAA+ disaggregase ClpL from
MeSH term(s)	Humans ; Animals ; Listeria monocytogenes ; Cell Death ; Estrus ; Food ; HSP70 Heat-Shock Proteins ; Neural Tube Defects
Chemical Substances	HSP70 Heat-Shock Proteins
Language	English
Publishing date	2024-04-10
Publishing country	England
Document type	Journal Article
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.92746
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Article ; Online: Antibacterial peptide CyclomarinA creates toxicity by deregulating the Mycobacterium tuberculosis ClpC1-ClpP1P2 protease.

Taylor, Gabrielle / Frommherz, Yannick / Katikaridis, Panagiotis / Layer, Dominik / Sinning, Irmgard / Carroni, Marta / Weber-Ban, Eilika / Mogk, Axel

The Journal of biological chemistry

2022 Volume 298, Issue 8, Page(s) 102202

Abstract: The ring-forming AAA+ hexamer ClpC1 associates with the peptidase ClpP1P2 to form a central ATP-driven protease in Mycobacterium tuberculosis (Mtb). ClpC1 is essential for Mtb viability and has been identified as the target of antibacterial peptides like ...

Abstract	The ring-forming AAA+ hexamer ClpC1 associates with the peptidase ClpP1P2 to form a central ATP-driven protease in Mycobacterium tuberculosis (Mtb). ClpC1 is essential for Mtb viability and has been identified as the target of antibacterial peptides like CyclomarinA (CymA) that exhibit strong toxicity toward Mtb. The mechanistic actions of these drugs are poorly understood. Here, we dissected how ClpC1 activity is controlled and how this control is deregulated by CymA. We show that ClpC1 exists in diverse activity states correlating with its assembly. The basal activity of ClpC1 is low, as it predominantly exists in an inactive nonhexameric resting state. We show that CymA stimulates ClpC1 activity by promoting formation of supercomplexes composed of multiple ClpC1 hexameric rings, enhancing ClpC1-ClpP1P2 degradation activity toward various substrates. Both the ClpC1 resting state and the CymA-induced alternative assembly state rely on interactions between the ClpC1 coiled-coil middle domains (MDs). Accordingly, we found that mutation of the conserved aromatic F444 residue located at the MD tip blocks MD interactions and prevents assembly into higher order complexes, thereby leading to constitutive ClpC1 hexamer formation. We demonstrate that this assembly state exhibits the highest ATPase and proteolytic activities, yet its heterologous expression in Escherichia coli is toxic, indicating that the formation of such a state must be tightly controlled. Taken together, these findings define the basis of control of ClpC1 activity and show how ClpC1 overactivation by an antibacterial drug generates toxicity.
MeSH term(s)	Anti-Bacterial Agents/pharmacology ; Bacterial Proteins/chemistry ; Bacterial Proteins/metabolism ; Endopeptidase Clp/chemistry ; Endopeptidase Clp/metabolism ; Endopeptidases/metabolism ; Escherichia coli/metabolism ; Heat-Shock Proteins/chemistry ; Heat-Shock Proteins/metabolism ; Mycobacterium tuberculosis/enzymology ; Mycobacterium tuberculosis/metabolism ; Oligopeptides/pharmacology ; Peptide Hydrolases/metabolism ; Peptides/metabolism
Chemical Substances	Anti-Bacterial Agents ; Bacterial Proteins ; ClpC1 protein, Mycobacterium tuberculosis ; Heat-Shock Proteins ; Oligopeptides ; Peptides ; cyclomarin A ; Endopeptidases (EC 3.4.-) ; Peptide Hydrolases (EC 3.4.-) ; Endopeptidase Clp (EC 3.4.21.92)
Language	English
Publishing date	2022-06-26
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2022.102202
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Article ; Online: ClpG Provides Increased Heat Resistance by Acting as Superior Disaggregase.

Katikaridis, Panagiotis / Meins, Lena / Kamal, Shady Mansour / Römling, Ute / Mogk, Axel

Biomolecules

2019 Volume 9, Issue 12

Abstract: Elevation of temperature within and above the physiological limit causes the unfolding and aggregation of cellular proteins, which can ultimately lead to cell death. Bacteria are therefore equipped with Hsp100 disaggregation machines that revert the ... ...

Abstract	Elevation of temperature within and above the physiological limit causes the unfolding and aggregation of cellular proteins, which can ultimately lead to cell death. Bacteria are therefore equipped with Hsp100 disaggregation machines that revert the aggregation process and reactivate proteins otherwise lost by aggregation. In Gram-negative bacteria, two disaggregation systems have been described: the widespread ClpB disaggregase, which requires cooperation with an Hsp70 chaperone, and the standalone ClpG disaggregase. ClpG co-exists with ClpB in selected bacteria and provides superior heat resistance. Here, we compared the activities of both disaggregases towards diverse model substrates aggregated in vitro and in vivo at different temperatures. We show that ClpG exhibits robust activity towards all disordered aggregates, whereas ClpB acts poorly on the protein aggregates formed at very high temperatures. Extreme temperatures are expected not only to cause extended protein unfolding, but also to result in an accelerated formation of protein aggregates with potentially altered chemical and physical parameters, including increased stability. We show that ClpG exerts higher threading forces as compared to ClpB, likely enabling ClpG to process "tight" aggregates formed during severe heat stress. This defines ClpG as a more powerful disaggregase and mechanistically explains how ClpG provides increased heat resistance.
MeSH term(s)	Antigens, Bacterial/genetics ; Antigens, Bacterial/metabolism ; Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Endopeptidase Clp/genetics ; Endopeptidase Clp/metabolism ; Escherichia coli/growth & development ; Escherichia coli/metabolism ; Escherichia coli Proteins/genetics ; Escherichia coli Proteins/metabolism ; Heat-Shock Proteins/genetics ; Heat-Shock Proteins/metabolism ; Hot Temperature ; Protein Aggregates ; Protein Unfolding ; Pseudomonas aeruginosa/growth & development ; Pseudomonas aeruginosa/metabolism ; Stress, Physiological
Chemical Substances	Antigens, Bacterial ; Bacterial Proteins ; Escherichia coli Proteins ; Heat-Shock Proteins ; Protein Aggregates ; clpG protein, E coli (144998-09-4) ; Endopeptidase Clp (EC 3.4.21.92) ; ClpB protein, E coli (EC 3.6.1.3)
Language	English
Publishing date	2019-12-02
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2701262-1
ISSN	2218-273X ; 2218-273X
ISSN (online)	2218-273X
ISSN	2218-273X
DOI	10.3390/biom9120815
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Article ; Online: A recently isolated human commensal Escherichia coli ST10 clone member mediates enhanced thermotolerance and tetrathionate respiration on a P1 phage-derived IncY plasmid.

Kamal, Shady Mansour / Cimdins-Ahne, Annika / Lee, Changhan / Li, Fengyang / Martín-Rodríguez, Alberto J / Seferbekova, Zaira / Afasizhev, Robert / Wami, Haleluya Tesfaye / Katikaridis, Panagiotis / Meins, Lena / Lünsdorf, Heinrich / Dobrindt, Ulrich / Mogk, Axel / Römling, Ute

Molecular microbiology

2020 Volume 115, Issue 2, Page(s) 255–271

Abstract: The ubiquitous human commensal Escherichia coli has been well investigated through its model representative E. coli K-12. In this work, we initially characterized E. coli Fec10, a recently isolated human commensal strain of phylogroup A/sequence type ... ...

Abstract	The ubiquitous human commensal Escherichia coli has been well investigated through its model representative E. coli K-12. In this work, we initially characterized E. coli Fec10, a recently isolated human commensal strain of phylogroup A/sequence type ST10. Compared to E. coli K-12, the 4.88 Mbp Fec10 genome is characterized by distinct single-nucleotide polymorphisms and acquisition of genomic islands. In addition, E. coli Fec10 possesses a 155.86 kbp IncY plasmid, a composite element based on phage P1. pFec10 harbours multiple cargo genes such as coding for a tetrathionate reductase and its corresponding regulatory two-component system. Among the cargo genes is also the Transmissible Locus of Protein Quality Control (TLPQC), which mediates tolerance to lethal temperatures in bacteria. The disaggregase ClpG
MeSH term(s)	Bacteriophage P1/genetics ; Bacteriophages/genetics ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Genome, Bacterial ; Genomic Islands ; Humans ; Oxygen Consumption/physiology ; Plasmids/genetics ; Symbiosis/physiology ; Thermotolerance/genetics ; Thermotolerance/physiology
Language	English
Publishing date	2020-10-12
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	619315-8
ISSN	1365-2958 ; 0950-382X
ISSN (online)	1365-2958
ISSN	0950-382X
DOI	10.1111/mmi.14614
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Article ; Online: A recently isolated human commensal Escherichia coli ST10 clone member mediates enhanced thermotolerance and tetrathionate respiration on a P1 phage derived IncY plasmid.

Kamal, Shady Mansour / Cimdins-Ahne, Annika / Lee, Changhan / Li, Fengyang / Martin-Rodriguez, Alberto J / Seferbekova, Zaira / Afasizhev, Robert / Tesfaye Wami, Haleluya / Katikaridis, Panagiotis / Meins, Lena / Lünsdorf, Heinrich / Dobrindt, Ulrich / Mogk, Axel / Römling, Ute

Molecular microbiology ; England

2020

Abstract	The ubiquitous human commensal Escherichia coli has been well investigated through its model representative E. coli K-12. In this work, we initially characterized E. coli Fec10, a recently isolated human commensal strain of phylogroup A/sequence type ST10. Compared to E. coli K-12, the 4.88 Mbp Fec10 genome is characterized by distinct single nucleotide polymorphisms and acquisition of genomic islands. In addition, E. coli Fec10 possesses a 155.86 kbp IncY plasmid, a composite element based on phage P1. pFec10 codes for a variety of cargo genes such as a tetrathionate reductase and its corresponding regulatory two-component system. Among cargo gene products is also the Transmissible Locus of Protein Quality Control (TLPQC), which mediates tolerance to lethal temperatures in bacteria. The disaggregase ClpGGI of TLPQC constitutes a major determinant of thermotolerance of E. coli Fec10. We confirm stand-alone disaggregation activity, but observe distinct biochemical characteristics of ClpGGI-Fec10 compared to the nearly identical Pseudomonas aeruginosa ClpGGI-SG17M. Furthermore, we observed a unique contribution of ClpGGI-Fec10 to the exquisite thermotolerance of E. coli Fec10 suggesting functional differences between both disaggregases in vivo. Detection of thermotolerance in 10% of human commensal E. coli isolates suggests successful establishment of food-borne heat resistant strains in the human gut.
Keywords	Escherichia coli ; IncY plasmid ; disaggregase ClpG ; phylogenetic analysis ; tetrathionate respiration ; thermotolerance
Language	English
Publishing date	2020-09-28
Publisher	Wiley
Publishing country	de
Document type	Article ; Online
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Article ; Online: Structural basis of aggregate binding by the AAA+ disaggregase ClpG.

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Article: Resisting the Heat: Bacterial Disaggregases Rescue Cells From Devastating Protein Aggregation.

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Article ; Online: Basic mechanism of the autonomous ClpG disaggregase.

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Article ; Online: The

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Article ; Online: Antibacterial peptide CyclomarinA creates toxicity by deregulating the Mycobacterium tuberculosis ClpC1-ClpP1P2 protease.

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Article ; Online: ClpG Provides Increased Heat Resistance by Acting as Superior Disaggregase.

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Article ; Online: A recently isolated human commensal Escherichia coli ST10 clone member mediates enhanced thermotolerance and tetrathionate respiration on a P1 phage-derived IncY plasmid.

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Article ; Online: A recently isolated human commensal Escherichia coli ST10 clone member mediates enhanced thermotolerance and tetrathionate respiration on a P1 phage derived IncY plasmid.

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