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  • 1
    Online Resource
    Online Resource
    Cham :Springer International Publishing AG,
    Keywords: Bacteriology. ; Electronic books.
    Type of Medium: Online Resource
    Pages: 1 online resource (457 pages)
    Edition: 1st ed.
    ISBN: 9783319530475
    Series Statement: Subcellular Biochemistry Series ; v.84
    DDC: 579.3
    Language: English
    Note: Intro -- Preface -- Contents -- About the Editors -- Selected Publications -- Chapter 1: Overview of the Diverse Roles of Bacterial and Archaeal Cytoskeletons -- Introduction -- Proteins that Form the Filaments -- Prokaryotic Cytokinesis -- Cell Constriction by a Ring of FtsZ Filaments -- Control of FtsZ Filaments by Associated Proteins -- Restriction of Z Ring Assembly to Mid-Cell -- Prevention of Ring Assembly Near the Poles -- Constriction by ESCRT-III-Like Filaments -- DNA Segregation -- Segregation of Plasmids by Actin-Like Filaments -- Segregation of Plasmids and Phage by Tubulin-Like TubZ -- Segregation of Chromosomal DNA or Plasmids by WACAs -- Cell Shape Determination -- Actin-Like MreB in Rod-Shaped Cells -- Filamentous Proteins That Promote Curvature -- Organisation of Intracellular Membrane Compartments -- Evolutionary Relationships -- References -- Website -- Chapter 2: E. coli Cell Cycle Machinery -- Overview of Cell Cycle Regulation - Two Key Proteins -- DnaA and Initiation of Replication -- FtsZ and the Z Ring -- Components of the Cytokinetic Machinery - Cell Division Genes -- Assembly of the Z Rings -- FtsZ and Tubulin Form Dynamic Structures -- CCTP - High Affinity Through Polymerization Driven Avidity -- Membrane-Tethered FtsZ Filaments Coalesce at Midcell with the Aid of Zap Proteins -- Structure of the Z Ring -- In Vitro Reconstruction -- Additional Roles of the Z Ring -- Spatial Regulation of the Z Ring -- Min System -- Min Oscillation -- MinC/MinD Antagonism of Z Ring Formation -- Min and DNA Segregation -- Nucleoid Occlusion and SlmA -- Ter Linkage -- Overlap in Spatial Regulation -- From Z Ring to Divisome, Recruitment and Activation -- Downstream Proteins and Septal PG Synthesis -- FtsEX -- FtsK -- FtsQ, FtsL and FtsB -- FtsW -- FtsI -- FtsN -- Septal PG Machine -- Recruitment of Divisome Components to the Z Ring. , Depletion Studies Leading to a Linear Dependency Pathway -- Lessons from Fusions Leading to Forced Localization -- Bypass Mutations Suggest Some Components Are Core Whereas Others Are Non-core -- Role of FtsA and ZipA in Recruitment of Downstream Proteins -- The Role of FtsN in Activation of the Divisome -- Enigmatic Role of MreB and the Cell Elongation System in Cytokinesis -- Splitting the Septum -- Cell Size Regulation -- Metabolic Regulation -- Mutations Reducing Cell Size -- Size Control and the Cell Cycle -- Summary -- References -- Chapter 3: Cell Cycle Machinery in Bacillus subtilis -- Introduction to B. subtilis -- MreB and the Cell Elongation Machinery -- Organization of the B. subtilis Cell Wall -- B. subtilis Has Three Actin Like MreB Homologues -- Filaments, Foci and Movement -- A Complex Web of Interactions Between MreB Proteins and Cell Wall Effectors -- The Future -- FtsZ and the Cell Division Machinery -- Biochemical Properties of FtsZ -- FtsZ Visualization During Growth and Sporulation of B. subtilis -- The B. subtilis Divisome -- Regulation of Z Ring Formation and Cell Division -- Nucleoid Occlusion (NO) -- The Min System -- Nutritional Regulation of Cell Division -- Z Rings and Cell Division During Sporulation -- FtsZ Inhibitors as Potential Antibiotics -- L-Form (Cell Wall Deficient) Bacteria -- The Future -- References -- Chapter 4: Cytoskeletal Proteins in Caulobacter crescentus: Spatial Orchestrators of Cell Cycle Progression, Development, and Cell Shape -- The Caulobacter crescentus Life Cycle -- PopZ: Centromere Anchoring and Polar Organization -- PopZ Localization and Function in Cells -- Assembly Properties of PopZ -- PopZ: Unanswered Questions -- ParA and the Chromosome Segregation Machinery -- ParABS: Localization and Function in Cells -- Mechanism of ParABS-Mediated Chromosome Segregation. , Ensuring Robust Chromosome Segregation: ParABS and Beyond -- FtsZ: The Orchestrator of Cytokinesis -- FtsZ Domain Architecture and Function -- Z-ring Structure In Vivo -- FtsZ Function Over the Cell Cycle -- Force Generation and FtsZ Filament Curvature -- Cell Cycle Regulation of FtsZ Levels -- Positioning of the Z-ring in Coordination with DNA Segregation -- Metabolic Regulation of FtsZ Function -- MreB: Regulating Cell Shape and Polarity -- Regulation and Dynamics of MreB Localization -- MreB and C. crescentus Morphogenesis -- MreB and Polar Development -- MreB: Unanswered Questions -- Crescentin and Cell Curvature -- Crescentin Localization and Assembly Properties -- Crescentin-Mediated Cell Curvature: Mechanical Regulation of Peptidoglycan Synthesis -- Crescentin: Unanswered Questions -- CTP Synthase: Co-opting a Metabolic Enzyme to Define Cell Shape -- CtpS Localization and Role in Cell Curvature -- Assembly Properties of CtpS -- CtpS: Unanswered Questions -- Bactofilins: Scaffolds for Stalk Morphogenesis -- Function and Localization of Bactofilins -- Assembly Properties of Bactofilins -- C. crescentus Cytoskeletons: Future Perspectives -- References -- Chapter 5: FtsZ Constriction Force - Curved Protofilaments Bending Membranes -- Introduction -- Straight pfs and Minirings -- The Intermediate Curved pf Conformation -- What Induces the Transition from Straight to Curved pfs? -- Curved pfs Can Bend Membranes and Generate a Constriction Force -- FtsZ pfs Are Mechanically Rigid -- In Vitro Systems Reconstituted with FtsZ and FtsA -- Sliding pfs - Do They Generate Constriction or Just Accommodate It? -- Constriction Force by Partial Z Rings -- The pf Substructure of Z Rings - Ribbons or Scattered? -- The Spacing of pfs in the Ribbons -- The pf Substructure of Z Rings - Continuous or Patchy? -- Z-Ring Assembly and Initial Constriction. , The Final Step of Septum Closure -- References -- Chapter 6: Intermediate Filaments Supporting Cell Shape and Growth in Bacteria -- Introduction -- What Are Eukaryote Intermediate Filaments? -- Intermediate Filament Proteins Are Coiled-Coil Proteins -- Both Heptad and Hendecad Repeats Are Found in Eukaryote IF Proteins -- Structure of Eukaryote IF Proteins -- Higher Order Assemblies of Eukaryote IF Proteins -- Eukaryote IF Filaments in the Cellular Environment -- Mechanical Characteristics of IF Filaments -- Dynamics of Eukaryote IFs Is Controlled by Post-translational Modifications -- Bacterial Intermediate Filament-Like Proteins -- Crescentin, the First Identified Bacterial IF-Like Protein -- The Domain Organisation of Crescentin and Eukaryote IFs Are Very Similar -- Filament Formation of Crescentin in vitro and in vivo -- Dynamics of Crescentin in Its Cellular Environment -- Mechanical Properties of Crescentin -- What Is the Biological Function of Crescentin Dependent Cell Curvature? -- An Extended IF Family -- Novel Structural Characteristics of IF-Like Proteins: FilP and Scy from Streptomyces -- Assemblies of FilP and Scy in vitro -- Both Scy and FilP Support Filamentous Growth in Streptomyces -- Streptomyces - Polar Growth with Suspended Cell Division -- Growth at One Pole Is Prevalent in the Orders Actinomycetales and Rhizobiales -- The Essential Polarity Determinant, DivIVA -- Sustained Polar Growth in the Filamentous Streptomyces Is Orchestrated by a Multi-protein Assembly, the Tip Organising Centre (TIPOC), Including the IF-Like Proteins Scy and FilP -- FilP Supports Hyphal Mechanics During Growth -- Scy Is a Molecular Organiser at the Hyphal Tip -- Is Synchronous Cell Division Orchestrated from the TIPOC? -- Is There a Case for an Extended IF-Like Family? -- Bacterial Coiled-Coil Rich Proteins -- Conclusions -- References. , Chapter 7: FtsZ-ring Architecture and Its Control by MinCD -- Introduction -- The Divisome -- Fts Proteins -- FtsA Protein -- FtsZ Protein -- Z-ring Structure and Constriction Mechanism -- Spatiotemporal Regulation of Z-ring Assembly -- Nucleoid Occlusion - Protecting from Incision -- Min Systems in Gram Negative and Gram Positive Bacteria -- Regulation of Z-ring Position in Spherical Bacteria -- Alternative Regulators of Z-ring Position -- MipZ -- PomZ -- MapZ -- SsgAB -- The Min System in Rod-Shaped Bacteria -- MinC Dimers -- MinD Dimers -- MinE Activates MinD ATPase -- Structure and Activity of MinCD -- Molecular Interactions -- MinC-MinD form Bipolar Copolymers in vitro and in cells -- Structure of FtsZ-rings in vivo -- Z-ring Tethering to Membrane -- FtsA -- Essential Role of FtsA in E. coli -- Many Ways to Connect FtsZ to the Membrane -- Assembly of the Divisome -- Discovery of the Z-ring Using Immuno-Gold and GFP Imaging -- Z-ring Models -- A Model of the Z-ring from PALM Imaging -- The FtsZ-ring May Appear to Be Discontinuous -- STED -- 3D-SIM -- FRAP -- Effects of FtsZ-Bundling Proteins on the Ring Structure -- Limitations of FLM for the Investigation of the FtsZ-ring Structure -- CryoEM Studies of Z-ring Structure -- First CryoEM Study of Z-ring Structure -- More CryoEM Studies of Z-ring Structure -- Effects of the Missing Wedge of CryoET -- In vitro Z-ring Reconstitution Experiments -- Membrane Constriction by FtsZ-MTS -- Liposome Constriction by FtsZ/FtsA -- Rings of Both FtsZ and FtsA Filaments? -- FtsZ and FtsA Reconstituted on Flat Membranes -- 3D Structure of Reconstituted Rings in Liposomes -- Possible Drivers of Constriction -- Role of FtsA in Constriction -- Role of Nucleotides During Constriction -- Conclusions and Future Directions -- References -- Chapter 8: Bacterial Actins -- Introduction -- MamK Aligns Magnetosomes. , MamK Forms Cytoskeletal Filaments.
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 42 (2001), S. 0 
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Fluorescent polyclonal antibodies specific for MukB have been used to study its localization in Escherichia coli. In wild-type cells, the MukB protein appeared as a limited number of oblong shapes embracing the nucleoid. MukB remained associated with the nucleoid in the absence of DNA replication. The centre of gravity of the dispersed MukB signal initially localized near mid-cell, but moved to approximately quarter positions well before the termination of DNA replication and its subsequent reinitiation. Because MukB had been reported to bind to FtsZ and to its eukaryotic homologue tubulin in vitro, cells were co-labelled with MukB- and FtsZ-specific fluorophores. No co-localization of MukB with polymerized FtsZ (the FtsZ ring) was observed at any time during the cell cycle. A possible role for MukB in preventing premature FtsZ polymerization and in DNA folding that might assist DNA segregation is discussed.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 52 (2004), S. 0 
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Prokaryotic cell division occurs through the formation of a septum, which in Escherichia coli requires coordination of the invagination of the inner membrane, biosynthesis of peptidoglycan and constriction of the outer membrane. FtsN is an essential cell division protein and forms part of the divisome, a putative complex of proteins located in the cytoplasmic membrane. Structural analyses of FtsN by nuclear magnetic resonance (NMR) reveals an RNP-like fold at the C-terminus (comprising residues 243–319), which has significant sequence homology to a peptidoglycan-binding domain. Sequential deletion mutagenesis in combination with NMR shows that the remaining of the periplasmic region of FtsN is unfolded, with the exception of three short, only partially formed helices following the trans-membrane helix. Based on these findings we propose a model in which FtsN, anchored in the inner membrane, bridges over to the peptidoglycan layer, thereby enabling the coordination of the divisome and the murein-shaping machinery in the periplasm.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 53 (2004), S. 0 
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Prokaryotic chromosomes and plasmids encode partitioning systems that are required for DNA segregation at cell division. The plasmid partitioning loci encode two proteins, ParA and ParB, and a cis-acting centromere-like site denoted parS. The chromosomally encoded homologues of ParA and ParB, Soj and Spo0J, play an active role in chromosome segregation during bacterial cell division and sporulation. Spo0J is a DNA-binding protein that binds to parS sites in vivo. We have solved the X-ray crystal structure of a C-terminally truncated Spo0J (amino acids 1–222) from Thermus thermophilus to 2.3 Å resolution by multiwavelength anomalous dispersion. It is a DNA-binding protein with structural similarity to the helix–turn–helix (HTH) motif of the lambda repressor DNA-binding domain. The crystal structure is an antiparallel dimer with the recognition α-helices of the HTH motifs of each monomer separated by a distance of 34 Å corresponding to the length of the helical repeat of B-DNA. Sedimentation velocity and equilibrium ultracentrifugation studies show that full-length Spo0J exists in a monomer–dimer equilibrium in solution and that Spo0J1–222 is exclusively monomeric. Sedimentation of the C-terminal domain of Spo0J shows it to be exclusively dimeric, confirming that the C-terminus is the primary dimerization domain. We hypothesize that the C-terminus mediates dimerization of Spo0J, thereby effectively increasing the local concentration of the N-termini, which most probably dimerize, as shown by our structure, upon binding to a cognate parS site.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1545-9985
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] The bacterial septum-located DNA translocase FtsK coordinates circular chromosome segregation with cell division. Rapid translocation of DNA by FtsK is directed by 8-base-pair DNA motifs (KOPS), so that newly replicated termini are brought together at the developing septum, thereby facilitating ...
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature structural & molecular biology 11 (2004), S. 1243-1250 
    ISSN: 1545-9985
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] The prokaryotic tubulin homolog FtsZ polymerizes into a ring structure essential for bacterial cell division. We have used refolded FtsZ to crystallize a tubulin-like protofilament. The N- and C-terminal domains of two consecutive subunits in the filament assemble to form the GTPase site, with the ...
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    [s.l.] : Macmillan Magazines Ltd.
    Nature 391 (1998), S. 203-206 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Bacterial cell division ends with septation, the constriction of the cell wall and cell membranes that leads to the formation of two daughter cells,. During septation, FtsZ, a protein of relative molecular mass 40,000 which is ubiquitous in eubacteria and is also found in archaea and ...
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    [s.l.] : Macmillian Magazines Ltd.
    Nature 413 (2001), S. 39-44 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] It was thought until recently that bacteria lack the actin or tubulin filament networks that organize eukaryotic cytoplasm. However, we show here that the bacterial MreB protein assembles into filaments with a subunit repeat similar to that of F-actin—the physiological polymer of eukaryotic ...
    Type of Medium: Electronic Resource
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  • 9
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The crystal structure of the 20S proteasome from the yeast Saccharomyces cerevisiae shows that its 28 protein subunits are arranged as an (α1...α7, β1...β7)2 complex in four stacked rings and occupy unique locations. The interior of the particle, which harbours the ...
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 444 (2006), S. 766-769 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Dynamins form a superfamily of large mechano-chemical GTPases that includes the classical dynamins and dynamin-like proteins (DLPs). They are found throughout the Eukarya, functioning in core cellular processes such as endocytosis and organelle division. Many bacteria are predicted by ...
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