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Proteolysis In Plasmid DNA Stable Maintenance In Bacterial Cells.
A. Karłowicz, K. Węgrzyn, A. Dubiel, Malgorzata Ropelewska, I. Konieczny
Published 2016 · Biology, Medicine
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Plasmids, as extrachromosomal genetic elements, need to work out strategies that promote independent replication and stable maintenance in host bacterial cells. Their maintenance depends on constant formation and dissociation of nucleoprotein complexes formed on plasmid DNA. Plasmid replication initiation proteins (Rep) form specific complexes on direct repeats (iterons) localized within the plasmid replication origin. Formation of these complexes along with a strict control of Rep protein cellular concentration, quaternary structure, and activity, is essential for plasmid maintenance. Another important mechanism for maintenance of low-copy-number plasmids are the toxin-antitoxin (TA) post-segregational killing (psk) systems, which prevent plasmid loss from the bacterial cell population. In this mini review we discuss the importance of nucleoprotein complex processing by energy-dependent host proteases in plasmid DNA replication and plasmid type II toxin-antitoxin psk systems, and draw attention to the elusive role of DNA in this process.
This paper references
Formation of the preprimosome protects lambda O from RNA transcription-dependent proteolysis by ClpP/ClpX.
M. Żylicz (1998)
Genetic and functional analysis of the basic replicon of pPS10, a plasmid specific for Pseudomonas isolated from Pseudomonas syringae patovar savastanoi.
C. Nieto (1992)
The toxin-antitoxin system of the streptococcal plasmid pSM19035.
U. Zielenkiewicz (2005)
Interactions of CcdB with DNA Gyrase
E. M. Bahassi (1999)
Toxin-antitoxin systems homologous with relBE of Escherichia coli plasmid P307 are ubiquitous in prokaryotes.
H. Grønlund (1999)
Opposing effects of DNA on proteolysis of a replication initiator
S. Kubik (2012)
The ratio between CcdA and CcdB modulates the transcriptional repression of the ccd poison–antidote system
H. Afif (2001)
Dissociation kinetics of RepA dimers: implications for mechanisms of activation of DNA binding by chaperones
D. Chattoraj (1996)
Proteotoxic Stress Induces a Cell-Cycle Arrest by Stimulating Lon to Degrade the Replication Initiator DnaA
K. Jonas (2013)
Replication of plasmid RK2 in vitro by a DNA-membrane complex: evidence for initiation of replication and its coupling to transcription and translation.
J. Kornacki (1986)
The parDE operon of the broad-host-range plasmid RK2 specifies growth inhibition associated with plasmid loss.
R. Roberts (1994)
Replication initiator protein RepE of mini-F plasmid: functional differentiation between monomers (initiator) and dimers (autogenous repressor).
M. Ishiai (1994)
Negative regulation of pPS10 plasmid replication: origin pairing by zipping‐up DNA‐bound RepA monomers
F. Gasset-Rosa (2008)
The phage abortive infection system, ToxIN, functions as a protein–RNA toxin–antitoxin pair
P. C. Fineran (2009)
Toxin-antitoxin systems in bacteria and archaea.
Yoshihiro Yamaguchi (2011)
Helicase Delivery and Activation by DnaA and TrfA Proteins during the Initiation of Replication of the Broad Host Range Plasmid RK2*
I. Konieczny (1997)
Identification and purification of the Lon+ (capR+) gene product, a DNA-binding protein.
B. Zehnbauer (1981)
ATP-dependent Degradation of CcdA by Lon Protease
L. Van Melderen (1996)
A bacterial toxin inhibits DNA replication elongation through a direct interaction with the β sliding clamp.
Christopher D. Aakre (2013)
A phospho-signaling pathway controls the localization and activity of a protease complex critical for bacterial cell cycle progression.
Antonio A Iniesta (2006)
Identification of components of a new stability system of plasmid R1, ParD, that is close to the origin of replication of this plasmid
A. Bravo (2004)
Replication and Control of Circular Bacterial Plasmids
G. del Solar (1998)
Role of π Dimers in Coupling (“Handcuffing”) of Plasmid R6K's γ ori Iterons
S. Kunnimalaiyaan (2005)
Defective plasmid partition in ftsH mutants of Escherichia coli
T. Inagawa (2001)
Formation of the preprimosome protects λ O from RNA transcription-dependent proteolysis by ClpP/ClpX
M. Żylicz (1998)
ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal.
C. Lee (2001)
Activation of DNA binding by the monomeric form of the P1 replication initiator RepA by heat shock proteins DnaJ and DnaK.
S. Dasgupta (1993)
Roles of Escherichia coli heat shock proteins DnaK, DnaJ and GrpE in mini-F plasmid replication
Y. Kawasaki (2004)
The Plasmid RK2 Initiation Protein Binds to the Origin of Replication as a Monomer (*)
A. Toukdarian (1996)
Interactions of Kid–Kis toxin–antitoxin complexes with the parD operator-promoter region of plasmid R1 are piloted by the Kis antitoxin and tuned by the stoichiometry of Kid–Kis oligomers
M. Monti (2007)
YeeU enhances the bundling of cytoskeletal polymers of MreB and FtsZ, antagonizing the CbtA (YeeV) toxicity in Escherichia coli
H. Masuda (2012)
Origin pairing (‘handcuffing’) as a mode of negative control of P1 plasmid copy number
K. Park (2001)
The korB gene of broad host range plasmid RK2 is a major copy number control element which may act together with trfB by limiting trfA expression.
Christopher M Thomas (1984)
Multiple pathways of copy control of gamma replicon of R6K: mechanisms both dependent on and independent of cooperativity of interaction of tau protein with DNA affect the copy number.
A. Miron (1994)
Bacterial addiction module toxin Doc inhibits translation elongation through its association with the 30S ribosomal subunit
Mohan Liu (2008)
Cooperative Action of Escherichia coli ClpB Protein and DnaK Chaperone in the Activation of a Replication Initiation Protein*
I. Konieczny (2002)
Adapting proteostasis for disease
W. E. Balch (2008)
Forespore-specific transcription of the lonB gene during sporulation in Bacillus subtilis.
M. Serrano (2001)
Positive and negative roles of an initiator protein at an origin of replication.
M. Filutowicz (1986)
Conformation of a plasmid replication initiator protein affects its proteolysis by ClpXP system
M. Pierechod (2009)
Structural overview of toxin-antitoxin systems in infectious bacteria: a target for developing antimicrobial agents.
S. J. Park (2013)
Structural Changes in RepA, a Plasmid Replication Initiator, upon Binding to Origin DNA*
Teresa Díaz-López (2003)
AAA+ proteases: ATP-fueled machines of protein destruction.
R. Sauer (2011)
Processive degradation of proteins by the ATP-dependent Clp protease from Escherichia coli. Requirement for the multiple array of active sites in ClpP but not ATP hydrolysis.
M. W. Thompson (1994)
Conditional Activation of Toxin-Antitoxin Systems: Postsegregational Killing and Beyond.
A. M. Hernández-Arriaga (2014)
Two replication initiators - one mechanism for replication origin opening?
Elzbieta Zabrocka (2014)
Structural basis for nucleic acid and toxin recognition of the bacterial antitoxin CcdA
T. Madl (2006)
Cleavage of the antitoxin of the parD toxin-antitoxin system is determined by the ClpAP protease and is modulated by the relative ratio of the toxin and the antitoxin.
Elizabeth Diago-Navarro (2013)
Co‐operative autoregulation of a replication protein gene
A. Gammie (1991)
Modulation of pPS10 host range by DnaA
B. Maestro (2002)
Analysis of mutations in trfA, the replication initiation gene of the broad-host-range plasmid RK2.
J. Lin (1992)
Regulation of toxin-antitoxin systems by proteolysis.
I. Brzozowska (2013)
Plasmid RK2 toxin protein ParE: purification and interaction with the ParD antitoxin protein.
E. P. Johnson (1996)
DNA binding properties of purified replication initiator protein (Rep) encoded by plasmid pSC101.
S. Sugiura (1990)
The replication initiation protein of the broad-host-range plasmid RK2 is activated by the ClpX chaperone.
I. Konieczny (1997)
Transcription of repA, the gene of the initiation protein of the Pseudomonas plasmid pPS10, is autoregulated by interactions of the RepA protein at a symmetrical operator.
D. García de Viedma (1995)
Forespore - speci fi c transcription of the lonB gene during sporulation in Bacillus subtilis
Mechanism of autonomous control of the Escherichia coli F plasmid: different complexes of the initiator/repressor protein are bound to its operator and to an F plasmid replication origin.
L. Masson (1986)
The stable maintenance system pem of plasmid R100: degradation of PemI protein may allow PemK protein to inhibit cell growth.
S. Tsuchimoto (1992)
RelB and RelE of Escherichia coli Form a Tight Complex That Represses Transcription via the Ribbon–Helix–Helix Motif in RelB
M. Overgaard (2009)
A bacterial toxin inhibits DNA
C. D. Aakre (2013)
Tran - scription of repA , the gene of the initiation protein of the Pseudomonas plasmid pPS 10 , is autoregulated by interactions of the RepA protein at a symmetrical opera
D. Garcia de Viedma (1995)
Toxin-antitoxin Systems: Classification, Biological Function and Application in Biotechnology.
S. Ghafourian (2014)
Effects of Inorganic Polyphosphate on the Proteolytic and DNA-binding Activities of Lon in Escherichia coli*
Kazutaka Nomura (2004)
Plasmid replication initiator interactions with origin 13-mers and polymerase subunits contribute to strand-specific replisome assembly
Aleksandra Wawrzycka (2015)
The solution structure of ParD, the antidote of the ParDE toxin–antitoxin module, provides the structural basis for DNA and toxin binding
M. Oberer (2007)
Toxin-antitoxin systems: biology, identification, and application
S. J. Unterholzner (2013)
Adapting Proteostasis for Disease Intervention
W. Balch (2008)
ParE toxin encoded by the broad‐host‐range plasmid RK2 is an inhibitor of Escherichia coli gyrase
Y. Jiang (2002)
Regulation of Escherichia coli starvation sigma factor (sigma s) by ClpXP protease.
T. Schweder (1996)
ParE toxin encoded by the broadhost-range plasmid RK2 is an inhibitor of Escherichia coli
Y. Jiang (2002)
Degrons in protein substrates program the speed and operating efficiency of the AAA+ Lon proteolytic machine
E. Gur (2009)
Interactions of DnaA Proteins from Distantly Related Bacteria with the Replication Origin of the Broad Host Range Plasmid RK2*
R. Caspi (2000)
Role of Inorganic Polyphosphate in Promoting Ribosomal Protein Degradation by the Lon Protease in E. coli
A. Kuroda (2001)
Plasmid R6K replication control.
Sheryl A. Rakowski (2013)
A molecular chaperone, ClpA, functions like DnaK and DnaJ.
S. Wickner (1994)
P1 plasmid replication: multiple functions of RepA protein at the origin.
D. Chattoraj (1985)
A broad host range replicon with different requirements for replication initiation in three bacterial species
R. Caspi (2001)
Mini-F plasmid genes that couple host cell division to plasmid proliferation.
T. Ogura (1983)
Transcription in the trfA region of broad host range plasmid RK2 is regulated by trfB and korB
V. Shingler (2004)
The anti-toxin ParD of plasmid RK2 consists of two structurally distinct moieties and belongs to the ribbon-helix-helix family of DNA-binding proteins.
M. Oberer (2002)
Requirements for and Regulation of Origin Opening of Plasmid P1*
K. Park (1998)
Role of TrfA and DnaA Proteins in Origin Opening during Initiation of DNA Replication of the Broad Host Range Plasmid RK2*
I. Konieczny (1997)
ATP-dependent proteases of bacteria: recognition logic and operating principles.
T. A. Baker (2006)
The Caulobacter crescentus Homolog of DnaA (HdaA) Also Regulates the Proteolysis of the Replication Initiator Protein DnaA.
Richard Wargachuk (2015)
Vertebrate unfolded protein response: mammalian signaling pathways are conserved in Medaka fish.
T. Ishikawa (2011)
cation elongation through a direct interaction with the beta sliding clamp
N. Allali (2001)
RalR (a DNase) and RalA (a small RNA) form a type I toxin–antitoxin system in Escherichia coli
Yunxue Guo (2014)
Reconstitution of F Factor DNA Replication in Vitro with Purified Proteins*
S. Zzaman (2004)
Critical clamp loader processing by an essential AAA+ protease in Caulobacter crescentus
Robert H. Vass (2013)
Archaeal proteasomes and other regulatory proteases.
J. Maupin-Furlow (2005)
A Novel Type V TA System Where mRNA for Toxin GhoT is Cleaved by Antitoxin GhoS
Xiaoxue Wang (2012)
Biological and chemical approaches to diseases of proteostasis deficiency.
E. Powers (2009)
Crystal structure of the MazE/MazF complex: molecular bases of antidote-toxin recognition.
K. Kamada (2003)
Molecular Mechanisms of HipA-Mediated Multidrug Tolerance and Its Neutralization by HipB
M. Schumacher (2009)
DnaA boxes in the P1 plasmid origin: the effect of their position on the directionality of replication and plasmid copy number.
K. Park (2001)
Lon‐dependent proteolysis of CcdA is the key control for activation of CcdB in plasmid‐free segregant bacteria
L. Melderen (1994)
Regulated expression of a gene important for replication of plasmid F in E. coli.
L. Søgaard-Andersen (1984)
TrfA dimers play a role in copy-number control of RK2 replication.
A. Toukdarian (1998)
The antibiotic ADEP reprogrammes ClpP, switching it from a regulated to an uncontrolled protease
J. Kirstein (2009)
Rejuvenation of CcdB-poisoned gyrase by an intrinsically disordered protein domain.
N. de Jonge (2009)
Requirement of a plasmid-encoded protein for replication in vitro of plasmid R6K.
Manabu Inuzuka (1978)
The level of the pUB110 replication initiator protein is autoregulated, which provides an additional control for plasmid copy number.
A. K. Mueller (1995)
Comparison of ccd of F, parDE of RP4, and parD of R1 using a novel conditional replication control system of plasmid R1
R. B. Jensen (1995)
Addiction protein Phd of plasmid prophage P1 is a substrate of the ClpXP serine protease of Escherichia coli.
H. Lehnherr (1995)
ClpA mediates directional translocation of substrate proteins into the ClpP protease
B. G. Reid (2001)
The Escherichia coli replication inhibitor CspD is subject to growth‐regulated degradation by the Lon protease
Sina Langklotz (2011)
Origin pairing (‘handcuffing’) and unpairing in the control of P1 plasmid replication
N. Das (2004)
Genetic identification of two functional regions in the antitoxin of the parD killer system of plasmid R1.
S. Santos-Sierra (2002)
The ClpXP Protease Is Responsible for the Degradation of the Epsilon Antidote to the Zeta Toxin of the Streptococcal pSM19035 Plasmid
I. Brzozowska (2014)
Structural basis for nucleic acid and toxin recognition of the bacterial antitoxin CcdA.
T. Madl (2006)
P1 plasmid replication: measurement of initiator protein concentration in vivo.
J. Swack (1987)
Role of pi dimers in coupling ("handcuffing") of plasmid R6K's gamma ori iterons.
S. Kunnimalaiyaan (2005)
Txe, an endoribonuclease of the enterococcal Axe–Txe toxin–antitoxin system, cleaves mRNA and inhibits protein synthesis
Elizabeth M. Halvorsen (2011)
Spontaneous mutagenesis is elevated in protease‐defective cells
A. A. A. Al Mamun (2009)
Bacterial persistence and toxin-antitoxin loci.
K. Gerdes (2012)
A leucine zipper motif determines different functions in a DNA replication protein.
D. García de Viedma (1996)
This paper is referenced by
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