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  1. Article: Shape determination in Bacillus subtilis.

    Carballido-López, Rut / Formstone, Alex

    Current opinion in microbiology

    2007  Volume 10, Issue 6, Page(s) 611–616

    Abstract: The discovery of cytoskeletal elements in prokaryotes has dramatically changed the way we think about bacterial cell morphogenesis. The rod shape of Bacillus subtilis is maintained by the two major polymers (peptidoglycan and teichoic acids) of its thick ...

    Abstract The discovery of cytoskeletal elements in prokaryotes has dramatically changed the way we think about bacterial cell morphogenesis. The rod shape of Bacillus subtilis is maintained by the two major polymers (peptidoglycan and teichoic acids) of its thick cell wall and determined by the way these are inserted during growth. The current view is that the dynamic tubulin-like (FtsZ) and actin-like (MreB) cytoskeletons orchestrate, both in time and space, the assembly of macromolecular machineries that effect cell wall synthesis and hydrolysis during cell division and cell elongation, respectively.
    MeSH term(s) Bacillus subtilis/cytology ; Bacillus subtilis/genetics ; Bacillus subtilis/growth & development ; Bacillus subtilis/metabolism ; Cytoskeletal Proteins/metabolism ; Cytoskeleton/metabolism ; Gene Expression Regulation, Bacterial ; Peptidoglycan/metabolism ; Teichoic Acids/metabolism
    Chemical Substances Cytoskeletal Proteins ; Peptidoglycan ; Teichoic Acids
    Language English
    Publishing date 2007-12
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1418474-6
    ISSN 1879-0364 ; 1369-5274
    ISSN (online) 1879-0364
    ISSN 1369-5274
    DOI 10.1016/j.mib.2007.09.008
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: A magnesium-dependent mreB null mutant: implications for the role of mreB in Bacillus subtilis.

    Formstone, Alex / Errington, Jeffery

    Molecular microbiology

    2004  Volume 55, Issue 6, Page(s) 1646–1657

    Abstract: MreB shares a common prokaryotic ancestor with actin and is present in almost all rod-shaped bacteria. MreB proteins have been implicated in a range of important cell processes, including cell morphogenesis, chromosome segregation and cell polarity. The ... ...

    Abstract MreB shares a common prokaryotic ancestor with actin and is present in almost all rod-shaped bacteria. MreB proteins have been implicated in a range of important cell processes, including cell morphogenesis, chromosome segregation and cell polarity. The mreB gene frequently lies at the beginning of a cluster of genes, immediately upstream of the conserved mreC and mreD genes. RNA analysis showed that in Bacillus subtilis mreB is co-transcribed with mreC and that these genes form part of an operon under the control of a promoter(s) upstream of mreB. Construction of an in-frame deletion of mreB and its complementation by mreB(+) only, in trans, established that the gene is important for maintenance of cell width and cell viability under normal growth conditions, independent of polar effects on downstream genes. Remarkably, virtually normal growth was restored to the mreB null mutant in the presence of high concentrations of magnesium, especially when high concentrations of the osmoprotectant, sucrose were also present. Under these conditions, cells could be maintained in the complete absence of an mreB gene, with almost normal morphology. No detectable effect on chromosome segregation was evident in the mutant, nor was there an effect on the topology of nascent peptidoglycan insertion. A GFP-MreB fusion was used to look at the localization of MreB in live cells. The pattern of localization was similar to that previously described, but no tight linkage to nucleoid positioning was evident. Propagation of the mreB null mutant in the absence of magnesium and sucrose led to a progressive increase in cell width, culminating in cell lysis. Cell division was also perturbed but this effect may be secondary to the disturbance in cell width. These results suggest that the major role of MreB in B. subtilis lies in the control of cell diameter.
    MeSH term(s) Bacillus subtilis/chemistry ; Bacillus subtilis/genetics ; Bacillus subtilis/growth & development ; Bacillus subtilis/physiology ; Bacterial Proteins/genetics ; Bacterial Proteins/physiology ; Cell Wall/metabolism ; Chromosome Segregation ; Chromosomes, Bacterial/metabolism ; Gene Deletion ; Genes, Bacterial ; Genes, Essential ; Genes, Reporter ; Genetic Complementation Test ; Green Fluorescent Proteins/genetics ; Green Fluorescent Proteins/metabolism ; Magnesium/metabolism ; Morphogenesis/genetics ; Mutation ; Osmotic Pressure ; Peptidoglycan/metabolism ; Recombinant Fusion Proteins/analysis ; Recombinant Fusion Proteins/genetics ; Sequence Deletion ; Sucrose
    Chemical Substances Bacterial Proteins ; Peptidoglycan ; Recombinant Fusion Proteins ; Green Fluorescent Proteins (147336-22-9) ; Sucrose (57-50-1) ; Magnesium (I38ZP9992A)
    Language English
    Publishing date 2004-11-30
    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/j.1365-2958.2005.04506.x
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  3. Article ; Online: Localization and interactions of teichoic acid synthetic enzymes in Bacillus subtilis.

    Formstone, Alex / Carballido-López, Rut / Noirot, Philippe / Errington, Jeffery / Scheffers, Dirk-Jan

    Journal of bacteriology

    2007  Volume 190, Issue 5, Page(s) 1812–1821

    Abstract: The thick wall of gram-positive bacteria is a polymer meshwork composed predominantly of peptidoglycan (PG) and teichoic acids, both of which have a critical function in maintenance of the structural integrity and the shape of the cell. In Bacillus ... ...

    Abstract The thick wall of gram-positive bacteria is a polymer meshwork composed predominantly of peptidoglycan (PG) and teichoic acids, both of which have a critical function in maintenance of the structural integrity and the shape of the cell. In Bacillus subtilis 168 the major teichoic acid is covalently coupled to PG and is known as wall teichoic acid (WTA). Recently, PG insertion/degradation over the lateral wall has been shown to occur in a helical pattern. However, the spatial organization of WTA assembly and its relationship with cell shape and PG assembly are largely unknown. We have characterized the localization of green fluorescent protein fusions to proteins involved in several steps of WTA synthesis in B. subtilis: TagB, -F, -G, -H, and -O. All of these localized similarly to the inner side of the cytoplasmic membrane, in a pattern strikingly similar to that displayed by probes of nascent PG. Helix-like localization patterns are often attributable to the morphogenic cytoskeletal proteins of the MreB family. However, localization of the Tag proteins did not appear to be substantially affected by single disruption of any of the three MreB homologues of B. subtilis. Bacterial and yeast two-hybrid experiments revealed a complex network of interactions involving TagA, -B, -E, -F, -G, -H, and -O and the cell shape determinants MreC and MreD (encoded by the mreBCD operon and presumably involved in the spatial organization of PG synthesis). Taken together, our results suggest that, in B. subtilis at least, the synthesis and export of WTA precursors are mediated by a large multienzyme complex that may be associated with the PG-synthesizing machinery.
    MeSH term(s) ATP-Binding Cassette Transporters/genetics ; ATP-Binding Cassette Transporters/metabolism ; Bacillus subtilis/genetics ; Bacillus subtilis/metabolism ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Cell Membrane/metabolism ; Cell Wall/metabolism ; Green Fluorescent Proteins/genetics ; Green Fluorescent Proteins/metabolism ; Hydrolases/genetics ; Hydrolases/metabolism ; Lipoproteins/genetics ; Lipoproteins/metabolism ; Microscopy, Fluorescence ; Models, Biological ; Protein Binding ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/metabolism ; Teichoic Acids/biosynthesis ; Transferases (Other Substituted Phosphate Groups)/genetics ; Transferases (Other Substituted Phosphate Groups)/metabolism ; Two-Hybrid System Techniques
    Chemical Substances ATP-Binding Cassette Transporters ; Bacterial Proteins ; Lipoproteins ; MreC protein, Bacteria ; Recombinant Fusion Proteins ; TagA protein, bacteria ; Teichoic Acids ; tagG protein, Bacillus subtilis ; Green Fluorescent Proteins (147336-22-9) ; Transferases (Other Substituted Phosphate Groups) (EC 2.7.8.-) ; CDP glycerol glycerophosphotransferase (EC 2.7.8.12) ; Hydrolases (EC 3.-) ; tagH protein, Bacillus subtilis (EC 7.5.2.4)
    Language English
    Publishing date 2007-12-21
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2968-3
    ISSN 1098-5530 ; 0021-9193
    ISSN (online) 1098-5530
    ISSN 0021-9193
    DOI 10.1128/JB.01394-07
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  4. Article: Actin homolog MreBH governs cell morphogenesis by localization of the cell wall hydrolase LytE.

    Carballido-López, Rut / Formstone, Alex / Li, Ying / Ehrlich, S Dusko / Noirot, Philippe / Errington, Jeff

    Developmental cell

    2006  Volume 11, Issue 3, Page(s) 399–409

    Abstract: MreB proteins are bacterial actin homologs involved in cell morphogenesis and various other cellular processes. However, the effector proteins used by MreBs remain largely unknown. Bacillus subtilis has three MreB isoforms. Mbl and possibly MreB have ... ...

    Abstract MreB proteins are bacterial actin homologs involved in cell morphogenesis and various other cellular processes. However, the effector proteins used by MreBs remain largely unknown. Bacillus subtilis has three MreB isoforms. Mbl and possibly MreB have previously been shown to be implicated in cell wall synthesis. We have now found that the third isoform, MreBH, colocalizes with the two other MreB isoforms in B. subtilis and also has an important role in cell morphogenesis. MreBH can physically interact with a cell wall hydrolase, LytE, and is required for its helical pattern of extracellular localization. Moreover, lytE and mreBH mutants exhibit similar cell-wall-related defects. We propose that controlled elongation of rod-shaped B. subtilis depends on the coordination of cell wall synthesis and hydrolysis in helical tracts defined by MreB proteins. Our data also suggest that physical interactions with intracellular actin bundles can influence the later localization pattern of extracellular effectors.
    MeSH term(s) Actins/analysis ; Actins/metabolism ; Actins/physiology ; Bacillus subtilis/enzymology ; Bacillus subtilis/genetics ; Bacillus subtilis/growth & development ; Bacterial Proteins/metabolism ; Bacterial Proteins/physiology ; Cell Polarity ; Cell Wall/metabolism ; Cell Wall/physiology ; Chromosome Segregation ; Chromosomes, Bacterial ; Hydrolases/metabolism ; Magnesium/pharmacology ; Models, Biological ; Morphogenesis ; N-Acetylmuramoyl-L-alanine Amidase/metabolism ; N-Acetylmuramoyl-L-alanine Amidase/physiology
    Chemical Substances Actins ; Bacterial Proteins ; Hydrolases (EC 3.-) ; LytE protein, Bacillus subtilis (EC 3.5.1.28) ; N-Acetylmuramoyl-L-alanine Amidase (EC 3.5.1.28) ; Magnesium (I38ZP9992A)
    Language English
    Publishing date 2006-09
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2054967-2
    ISSN 1878-1551 ; 1534-5807
    ISSN (online) 1878-1551
    ISSN 1534-5807
    DOI 10.1016/j.devcel.2006.07.017
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