Poles apart: prokaryotic polar organelles and their spatial regulation, Cold Spring Harb. Perspect. Biol, vol.3, p.6809, 2011. ,
How do bacteria localize proteins to the cell pole?, J. Cell Sci, vol.127, pp.11-19, 2014. ,
Building the bacterial cell wall at the pole, Curr. Opin. Microbiol, vol.34, pp.53-59, 2016. ,
Recent advances on the development of bacterial poles, Trends Microbiol, vol.12, pp.518-525, 2004. ,
Asymmetric segregation of protein aggregates is associated with cellular aging and rejuvenation, Proc. Natl Acad. Sci. USA, vol.105, pp.3076-3081, 2008. ,
Quantitative and spatio-temporal features of protein aggregation in Escherichia coli and consequences on protein quality control and cellular ageing, EMBO J, vol.29, pp.910-923, 2010. ,
Nucleoid occlusion and bacterial cell division, Nat. Rev. Microbiol, vol.10, pp.8-12, 2012. ,
Localization of protein aggregation in Escherichia coli is governed by diffusion and nucleoid macromolecular crowding effect, PLoS Comput. Biol, vol.9, p.1003038, 2013. ,
URL : https://hal.archives-ouvertes.fr/hal-00798053
Localization of aggregating proteins in bacteria depends on the rate of addition, Front Microbiol, vol.5, p.418, 2014. ,
Segregation of molecules at cell division reveals native protein localization, Nat. Methods, vol.9, pp.480-482, 2012. ,
Cytoplasmic targeting of IpaC to the bacterial pole directs polar type III secretion in Shigella, EMBO J, vol.27, pp.447-457, 2008. ,
A genome-scale proteomic screen identifies a role for DnaK in chaperoning of polar autotransporters in Shigella, J. Bacteriol, vol.191, pp.6300-6311, 2009. ,
Splitsville: structural and functional insights into the dynamic bacterial Z ring, Nat. Rev. Microbiol, vol.14, pp.305-319, 2016. ,
Structural basis for the geometry-driven localization of a small protein, Proc. Natl Acad. Sci. USA, vol.112, pp.1908-1915, 2015. ,
Protein localization in Escherichia coli cells: comparison of the cytoplasmic membrane proteins ProP, LacY, ProW, AqpZ, MscS, and MscL, J. Bacteriol, vol.192, pp.912-924, 2010. ,
Spatiotemporal control of PopZ localization through cell cycle-coupled multimerization, J. Cell Biol, vol.201, pp.827-841, 2013. ,
Polar localization of the autotransporter family of large bacterial virulence proteins, J. Bacteriol, vol.188, pp.4841-4850, 2006. ,
Polar targeting of Shigella virulence factor IcsA in Enterobacteriacae and Vibrio, Proc. Natl Acad. Sci. USA, vol.98, pp.9871-9876, 2001. ,
DnaK functions as a central hub in the E. coli chaperone network, Cell Rep, vol.1, pp.251-264, 2012. ,
URL : https://hal.archives-ouvertes.fr/hal-00787591
Folding and purification of insoluble (inclusion body) proteins from Escherichia coli, Curr. Protoc. Protein Sci, vol.78, pp.1-30, 2014. ,
Caulobacter PopZ forms a polar subdomain dictating sequential changes in pole composition and function, Mol. Microbiol, vol.76, pp.173-189, 2010. ,
A polymeric protein anchors the chromosomal origin/ ParB complex at a bacterial cell pole, Cell, vol.134, pp.945-955, 2008. ,
The DnaK chaperone system of Escherichia coli: quaternary structures and interactions of the DnaK and GrpE components, J. Biol. Chem, vol.270, pp.2183-2189, 1995. ,
Visualization and functional analysis of the oligomeric states of Escherichia coli heat shock protein 70 (Hsp70/DnaK), Cell Stress Chaperon, vol.17, pp.313-327, 2012. ,
E. coli transports aggregated proteins to the poles by a specific and energy-dependent process, J. Mol. Biol, vol.392, pp.589-601, 2009. ,
Integrating protein homeostasis strategies in prokaryotes, Cold Spring Harb. Perspect. Biol, vol.3, p.4366, 2011. ,
ATPase-defective derivatives of Escherichia coli DnaK that behave differently with respect to ATP-induced conformational change and peptide release, J. Bacteriol, vol.183, pp.5482-5490, 2001. ,
The Hsp70 chaperone machines of Escherichia coli: a paradigm for the repartition of chaperone functions, Mol. Microbiol, vol.66, pp.840-857, 2007. ,
URL : https://hal.archives-ouvertes.fr/hal-00211365
Structural studies on the forward and reverse binding modes of peptides to the chaperone DnaK, J. Mol. Biol, vol.425, pp.2463-2479, 2013. ,
Entropy-driven spatial organization of highly confined polymers: lessons for the bacterial chromosome, Proc. Natl Acad. Sci. USA, vol.103, pp.12388-12393, 2006. ,
Physics of intracellular organization in bacteria, Annu Rev. Microbiol, vol.69, pp.361-379, 2015. ,
In vivo kinetics of segregation and polar retention of MS2-GFP-RNA complexes in Escherichia coli, Biophys. J, vol.106, pp.1928-1937, 2014. ,
The bacterial cytoplasm has glass-like properties and is fluidized by metabolic activity, Cell, vol.156, pp.183-194, 2014. ,
Structure of the complex of the colicin E2 R-domain and its BtuB receptor. The outer membrane colicin translocon, J. Biol. Chem, vol.282, pp.23163-23170, 2007. ,
Specific and potent inhibition of NAD + -dependent DNA ligase by pyridochromanones, J. Biol. Chem, vol.278, pp.39435-39442, 2003. ,
A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications, Nat. Biotechnol, vol.20, pp.87-90, 2002. ,
Unique peptide substrate binding properties of 110-kDa heatshock protein (Hsp110) determine its distinct chaperone activity, J. Biol. Chem, vol.287, pp.5661-5672, 2012. ,
Hsp70 chaperones: cellular functions and molecular mechanism, Cell Mol. Life Sci, vol.62, pp.670-684, 2005. ,
Type III secretion: building and operating a remarkable nanomachine, Trends Biochem Sci, vol.41, pp.175-189, 2016. ,
The spatial biology of transcription and translation in rapidly growing Escherichia coli, Front. Microbiol, vol.6, p.636, 2015. ,
A functional DnaK dimer is essential for the efficient interaction with Hsp40 heat shock protein, J. Biol. Chem, vol.290, pp.8849-8862, 2015. ,
Accurate prediction of DnaK-peptide binding via homology modelling and experimental data, PLoS Comput. Biol, vol.5, p.1000475, 2009. ,
Chaperone networking facilitates protein targeting to the bacterial cytoplasmic membrane, Biochim. Biophys. Acta, vol.1843, pp.1442-1456, 2014. ,
URL : https://hal.archives-ouvertes.fr/hal-00944970
The DnaK/DnaJ chaperone machinery of Salmonella enterica serovar Typhimurium is essential for invasion of epithelial cells and survival within macrophages, leading to systemic infection, Infect. Immun, vol.72, pp.1364-1373, 2004. ,
Chaperone release and unfolding of substrates in type III secretion, Nature, vol.437, pp.911-915, 2005. ,
Secretion of type III effectors into host cells in real time, Nat. Methods, vol.2, pp.959-965, 2005. ,
The Escherichia coli DjlA and CbpA proteins can substitute for DnaJ in DnaK-mediated protein disaggregation, J. Bacteriol, vol.186, pp.7236-7242, 2004. ,
Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains, Cell, vol.97, pp.755-765, 1999. ,
The djlA gene acts synergistically with dnaJ in promoting Escherichia coli growth, J. Bacteriol, vol.183, pp.5747-5750, 2001. ,
Extracellular association and cytoplasmic partitioning of the IpaB and IpaC invasins of S. flexneri, Cell, vol.79, pp.515-525, 1994. ,
Aging and death in an organism that reproduces by morphologically symmetric division, PLoS Biol, vol.3, p.45, 2005. ,
URL : https://hal.archives-ouvertes.fr/inserm-00080154
MicrobeJ, a tool for high throughput bacterial cell detection and quantitative analysis, Nat. Microbiol, vol.1, p.16077, 2016. ,
Robust single-particle tracking in live-cell time-lapse sequences, Nat. Methods, vol.5, pp.695-702, 2008. ,
A conserved loop in the ATPase domain of the DnaK chaperone is essential for stable binding of GrpE, Nat. Struct. Biol, vol.1, pp.95-101, 1994. ,
In vivo analysis of the overlapping functions of DnaK and trigger factor, EMBO Rep, vol.5, pp.195-200, 2004. ,
The heat-shock-regulated grpE gene of Escherichia coli is required for bacterial growth at all temperatures but is dispensable in certain mutant backgrounds, J. Bacteriol, vol.171, pp.2748-2755, 1989. ,
Scanning mutagenesis identifies amino acid residues essential for the in vivo activity of the Escherichia coli DnaJ (Hsp40) J-domain, Genetics, vol.162, pp.1045-1053, 2002. ,
Mutations of the molecular chaperone protein SecB which alter the interaction between SecB and maltose-binding protein, J. Biol. Chem, vol.268, pp.1590-1595, 1993. ,
The secretion of the Shigella flexneri Ipa invasins is activated by epithelial cells and controlled by IpaB and IpaD, EMBO J, vol.13, pp.5293-5302, 1994. ,
Secretion of Shigella flexneri Ipa invasins on contact with epithelial cells and subsequent entry of the bacterium into cells are growth stage dependent, Infect. Immun, vol.65, pp.774-782, 1997. ,
Acid-denatured Green Fluorescent Protein (GFP) as model substrate to study the chaperone activity of protein disulfide isomerase, Int J. Mol. Sci, vol.12, pp.4625-4636, 2011. ,