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D. Pandey, K. Gerdes (2005)
Toxin–antitoxin loci are highly abundant in free-living but lost from host-associated prokaryotesNucleic Acids Research, 33
J. Hurley, N. Woychik (2009)
Bacterial Toxin HigB Associates with Ribosomes and Mediates Translation-dependent mRNA Cleavage at A-rich Sites*The Journal of Biological Chemistry, 284
K. Pedersen, A. Zavialov, M. Pavlov, J. Elf, K. Gerdes, M. Ehrenberg (2003)
The Bacterial Toxin RelE Displays Codon-Specific Cleavage of mRNAs in the Ribosomal A SiteCell, 112
R. Leplae, Damien Geeraerts, Régis Hallez, Julien Guglielmini, P. Dreze, L. Melderen (2011)
Diversity of bacterial type II toxin–antitoxin systems: a comprehensive search and functional analysis of novel familiesNucleic Acids Research, 39
Y. Yamaguchi, Jung-Ho Park, M. Inouye (2009)
MqsR, a Crucial Regulator for Quorum Sensing and Biofilm Formation, Is a GCU-specific mRNA Interferase in Escherichia coli*The Journal of Biological Chemistry, 284
(2006)
Scaling and assessment of data quality
R. Magnuson (2007)
Hypothetical Functions of Toxin-Antitoxin SystemsJournal of Bacteriology, 189
Y. Yamaguchi, Jung-Ho Park, M. Inouye (2011)
Toxin-antitoxin systems in bacteria and archaea.Annual review of genetics, 45
Andres Ainelo, Hedvig Tamman, Margus Leppik, J. Remme, R. Hõrak (2016)
The toxin GraT inhibits ribosome biogenesisMolecular Microbiology, 100
(2010)
Acta Cryst
T. Ogura, S. Hiraga (1983)
Mini-F plasmid genes that couple host cell division to plasmid proliferation.Proceedings of the National Academy of Sciences of the United States of America, 80 15
Yajing Liang, Zengqiang Gao, Fei Wang, Yangli Zhang, Yuhui Dong, Quansheng Liu (2014)
Structural and Functional Characterization of Escherichia coli Toxin-Antitoxin Complex DinJ-YafQ*The Journal of Biological Chemistry, 289
Elsa Germain, Daniel Castro-Roa, N. Zenkin, K. Gerdes (2013)
Molecular mechanism of bacterial persistence by HipA.Molecular cell, 52 2
R. Page, W. Peti (2016)
Toxin-antitoxin systems in bacterial growth arrest and persistence.Nature chemical biology, 12 4
Yonglong Zhang, Junjie Zhang, K. Hoeflich, M. Ikura, Guoliang Qing, M. Inouye (2003)
MazF cleaves cellular mRNAs specifically at ACA to block protein synthesis in Escherichia coli.Molecular cell, 12 4
Hedvig Tamman, Andres Ainelo, Kadi Ainsaar, R. Hõrak (2013)
A Moderate Toxin, GraT, Modulates Growth Rate and Stress Tolerance of Pseudomonas putidaJournal of Bacteriology, 196
K. Gerdes, S. Christensen, A. Løbner‐Olesen (2005)
Prokaryotic toxin–antitoxin stress response lociNature Reviews Microbiology, 3
Daniel Castro-Roa, A. Garcia-Pino, Steven Gieter, N. Nuland, R. Loris, N. Zenkin (2013)
The Fic protein Doc uses an inverted substrate to phosphorylate and inactivate EF-TuNature chemical biology, 9
J. Whitaker (1963)
Determination of Molecular Weights of Proteins by Gel Filtration of Sephadex.Analytical Chemistry, 35
A. Hungler, A. Momin, K. Diederichs, S. Arold (2016)
ContaMiner and ContaBase: a webserver and database for early identification of unwantedly crystallized protein contaminantsJournal of Applied Crystallography, 49
Angela Cheverton, Bridget Gollan, Michal Przydacz, C. Wong, A. Mylona, S. Hare, S. Helaine (2016)
A Salmonella Toxin Promotes Persister Formation through Acetylation of tRNAMolecular Cell, 63
M. Dao‐Thi, L. Melderen, E. Genst, H. Afif, L. Buts, L. Wyns, R. Loris (2005)
Molecular basis of gyrase poisoning by the addiction toxin CcdB.Journal of molecular biology, 348 5
Régis Hallez, Damien Geeraerts, Yann Sterckx, Natacha Mine, R. Loris, L. Melderen (2010)
New toxins homologous to ParE belonging to three‐component toxin–antitoxin systems in Escherichia coli O157:H7Molecular Microbiology, 76
H. Mutschler, Maike Gebhardt, R. Shoeman, A. Meinhart (2011)
A Novel Mechanism of Programmed Cell Death in Bacteria by Toxin–Antitoxin Systems Corrupts Peptidoglycan SynthesisPLoS Biology, 9
(2011)
Nucleic Acids Res
M. Schureck, T. Maehigashi, S. Miles, Jhomar Marquez, Shein Cho, Rachel Erdman, C. Dunham (2013)
Structure of the Proteus vulgaris HigB-(HigA)2-HigB Toxin-Antitoxin Complex*The Journal of Biological Chemistry, 289
Elsa Germain, Mohammad Roghanian, K. Gerdes, Etienne Maisonneuve (2015)
Stochastic induction of persister cells by HipA through (p)ppGpp-mediated activation of mRNA endonucleasesProceedings of the National Academy of Sciences, 112
P. Bernard, M. Couturier (1992)
Cell killing by the F plasmid CcdB protein involves poisoning of DNA-topoisomerase II complexes.Journal of molecular biology, 226 3
B. Matthews (1968)
Solvent content of protein crystals.Journal of molecular biology, 33 2
R. Loris, A. Garcia-Pino (2014)
Disorder- and dynamics-based regulatory mechanisms in toxin-antitoxin modules.Chemical reviews, 114 13
K. Diederichs, P. Karplus (2013)
Better models by discarding data?Acta Crystallographica Section D: Biological Crystallography, 69
S. Christensen, K. Pedersen, F. Hansen, K. Gerdes (2003)
Toxin-antitoxin loci as stress-response-elements: ChpAK/MazF and ChpBK cleave translated RNAs and are counteracted by tmRNA.Journal of molecular biology, 332 4
(2011)
Molecules, 21, 790
Etienne Maisonneuve, K. Gerdes (2014)
Molecular Mechanisms Underlying Bacterial PersistersCell, 157
K. Kantardjieff, B. Rupp (2003)
Matthews coefficient probabilities: Improved estimates for unit cell contents of proteins, DNA, and protein–nucleic acid complex crystalsProtein Science, 12
M. Petoukhov, D. Franke, A. Shkumatov, Giancarlo Tria, A. Kikhney, M. Gajda, C. Gorba, H. Mertens, P. Konarev, D. Svergun
Electronic Reprint Applied Crystallography New Developments in the Atsas Program Package for Small-angle Scattering Data Analysis Applied Crystallography New Developments in the Atsas Program Package for Small-angle Scattering Data Analysis
D. Jurėnas, S. Chatterjee, A. Konijnenberg, F. Sobott, L. Droogmans, A. Garcia-Pino, L. Melderen (2017)
AtaT blocks translation initiation by N-acetylation of the initiator tRNAfMet.Nature chemical biology, 13 6
Breann Brown, Simina Grigoriu, Younghoon Kim, J. Arruda, Andrew Davenport, T. Wood, W. Peti, R. Page (2009)
Three Dimensional Structure of the MqsR:MqsA Complex: A Novel TA Pair Comprised of a Toxin Homologous to RelE and an Antitoxin with Unique PropertiesPLoS Pathogens, 5
M. Franklin, J. Cheung, M. Rudolph, F. Burshteyn, M. Cassidy, E. Gary, B. Hillerich, Zhong-Ke Yao, P. Carlier, M. Totrov, J. Love (2015)
Structural genomics for drug design against the pathogen Coxiella burnetiiProteins: Structure, 83
A. Ruangprasert, T. Maehigashi, S. Miles, Nisha Giridharan, Julie Liu, C. Dunham (2014)
Mechanisms of Toxin Inhibition and Transcriptional Repression by Escherichia coli DinJ-YafQ*The Journal of Biological Chemistry, 289
Jie Yuan, Yann Sterckx, L. Mitchenall, A. Maxwell, R. Loris, M. Waldor (2010)
Vibrio cholerae ParE2 Poisons DNA Gyrase via a Mechanism Distinct from Other Gyrase Inhibitors*The Journal of Biological Chemistry, 285
K. Gerdes, P. Rasmussen, S. Molin (1986)
Unique type of plasmid maintenance function: postsegregational killing of plasmid-free cells.Proceedings of the National Academy of Sciences of the United States of America, 83 10
Mikkel Christensen-Dalsgaard, K. Gerdes (2008)
Translation affects YoeB and MazF messenger RNA interferase activities by different mechanismsNucleic Acids Research, 36
P. Karplus, K. Diederichs (2012)
Linking Crystallographic Model and Data QualityScience, 336
(2005)
CCP 4 Newsl
Jingsi Yang, Ke Zhou, Peng Liu, Yuhui Dong, Zengqiang Gao, Jianjun Zhang, Quansheng Liu (2016)
Structural insight into the E. coli HigBA complex.Biochemical and biophysical research communications, 478 4
Meredith Prysak, Christopher Mozdzierz, A. Cook, Ling Zhu, Yonglong Zhang, M. Inouye, N. Woychik (2009)
Bacterial toxin YafQ is an endoribonuclease that associates with the ribosome and blocks translation elongation through sequence‐specific and frame‐dependent mRNA cleavageMolecular Microbiology, 71
A. Boggild, N. Sofos, K. Andersen, A. Feddersen, A. Easter, L. Passmore, D. Brodersen (2012)
The Crystal Structure of the Intact E. coli RelBE Toxin-Antitoxin Complex Provides the Structural Basis for Conditional CooperativityStructure(London, England:1993), 20
Yong Jiang, J. Pogliano, D. Helinski, I. Konieczny (2002)
ParE toxin encoded by the broad‐host‐range plasmid RK2 is an inhibitor of Escherichia coli gyraseMolecular Microbiology, 44
Alexander Harms, F. Stanger, P. Scheu, I. Jong, A. Goepfert, Timo Glatter, K. Gerdes, Tilman Schirmer, C. Dehio (2015)
Adenylylation of Gyrase and Topo IV by FicT Toxins Disrupts Bacterial DNA Topology.Cell reports, 12 9
Etienne Maisonneuve, Manuela Castro-Camargo, K. Gerdes (2013)
RETRACTED: (p)ppGpp Controls Bacterial Persistence by Stochastic Induction of Toxin-Antitoxin ActivityCell, 154
B. Kedzierska, F. Hayes (2016)
Emerging Roles of Toxin-Antitoxin Modules in Bacterial PathogenesisMolecules, 21
M. Arbing, S. Handelman, A. Kuzin, G. Verdon, Chi Wang, M. Su, Francesca Rothenbacher, M. Abashidze, Mohan Liu, J. Hurley, R. Xiao, T. Acton, M. Inouye, G. Montelione, N. Woychik, J. Hunt (2010)
Crystal structures of Phd-Doc, HigA, and YeeU establish multiple evolutionary links between microbial growth-regulating toxin-antitoxin systems.Structure, 18 8
U. Zielenkiewicz, P. Cegłowski (2005)
The Toxin-Antitoxin System of the Streptococcal Plasmid pSM19035Journal of Bacteriology, 187
Hedvig Tamman, Andres Ainelo, Mari Tagel, R. Hõrak (2015)
Stability of the GraA Antitoxin Depends on Growth Phase, ATP Level, and Global Regulator MexTJournal of Bacteriology, 198
The graTA operon from Pseudomonas putida encodes a toxin–antitoxin module with an unusually moderate toxin. Here, the production, SAXS analysis and crystallization of the antitoxin GraA, the GraTA complex and the complex of GraA with a 33 bp operator fragment are reported. GraA forms a homodimer in solution and crystallizes in space group P21, with unit‐cell parameters a = 66.9, b = 48.9, c = 62.7 Å, β = 92.6°. The crystals are likely to contain two GraA dimers in the asymmetric unit and diffract to 1.9 Å resolution. The GraTA complex forms a heterotetramer in solution. Crystals of the GraTA complex diffracted to 2.2 Å resolution and are most likely to contain a single heterotetrameric GraTA complex in the asymmetric unit. They belong to space group P41 or P43, with unit‐cell parameters a = b = 56.0, c = 128.2 Å. The GraA–operator complex consists of a 33 bp operator region that binds two GraA dimers. It crystallizes in space group P31 or P32, with unit‐cell parameters a = b = 105.6, c = 149.9 Å. These crystals diffract to 3.8 Å resolution.
Acta Crystallographica Section F – Wiley
Published: Jan 1, 2017
Keywords: ; ; ; ; ; ; ;
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