1. The dynamic nature of the bacterial cytoskeleton.

    Experientia. Basel 66(20):3353 (2009) PMID 19641848 PMCID PMC2810845

    Three of the four well-established bacterial cytoskeletal systems-the MreB, MinCDE, and FtsZ systems-undergo a variety of short-range and long-range dynamic behaviors. These include the cellular reorganization of the cytoskeletal elements, in which the proteins redistribute from a predominantly ...
  2. Assembly of the MreB-associated cytoskeletal ring of Escherichia coli.

    Molecular Microbiology 72(1):170 (2009) PMID 19220747

    The Escherichia coli actin homologue MreB is part of a helical cytoskeletal structure that winds around the cell between the two poles. It has been shown that MreB redistributes during the cell cycle to form circumferential ring structures that flank the cytokinetic FtsZ ring and appear to be as...
  3. New insights into the cellular organization of the RNA processing and degradation machinery of Escherichia coli.

    Molecular Microbiology 70(4):780 (2008) PMID 18990179

    Ribonuclease E (RNase E) is a component of the Escherichia coli RNA degradosome, a multiprotein complex that also includes RNA helicase B (RhlB), polynucleotide phosphorylase (PNPase) and enolase. The degradosome plays a key role in RNA processing and degradation. The degradosomal proteins are o...
  4. RNaseE and RNA helicase B play central roles in the cytoskeletal organization of the RNA degradosome.

    Journal of Biological Chemistry 283(20):13850 (2008) PMID 18337249 PMCID PMC2376217

    The RNA degradosome of Escherichia coli is a multiprotein complex that plays an essential role in normal RNA processing and decay. It was recently shown that the major degradosome constituents are organized in a coiled cytoskeletal-like structure that extends along the length of the cell. Here w...
  5. Cell shape determination in Escherichia coli.

    Current Opinion in Microbiology 10(6):606 (2007) PMID 17981077

    The rigid cell wall peptidoglycan (murein) is a single giant macromolecule whose shape determines the shape of the bacterial cell. Insight into morphogenetic mechanism(s) responsible for determining the shape of the murein sacculus itself has begun to emerge only in recent years. The discovery t...
  6. Duplication and segregation of the actin (MreB) cytoskeleton during the prokaryotic cell cycle.

    PNAS 104(45):17795 (2007) PMID 17978175 PMCID PMC2077029

    The bacterial actin homolog MreB exists as a single-copy helical cytoskeletal structure that extends between the two poles of rod-shaped bacteria. In this study, we show that equipartition of the MreB cytoskeleton into daughter cells is accomplished by division and segregation of the helical Mre...
  7. RNaseE and the other constituents of the RNA degradosome are components of the bacterial cytoskeleton.

    PNAS 104(5):1667 (2007) PMID 17242352 PMCID PMC1785250

    RNaseE is the main component of the RNA degradosome of Escherichia coli, which plays an essential role in RNA processing and decay. Localization studies showed that RNaseE and the other known degradosome components (RNA helicase B, polynucleotide phosphorylase, and enolase) are organized as heli...
  8. Cell shape determination inEscherichia coli

    Current Opinion in Microbiology 10(6):606 (2007)

    The rigid cell wall peptidoglycan (murein) is a single giant macromolecule whose shape determines the shape of the bacterial cell. Insight into morphogenetic mechanism(s) responsible for determining the shape of the murein sacculus itself has begun to emerge only in recent years. The discov...
  9. The bacterial cytoskeleton.

    Microbiology and Molecular Biology Reviews 70(3):729 (2006) PMID 16959967 PMCID PMC1594594

    In recent years it has been shown that bacteria contain a number of cytoskeletal structures. The bacterial cytoplasmic elements include homologs of the three major types of eukaryotic cytoskeletal proteins (actin, tubulin, and intermediate filament proteins) and a fourth group, the MinD-ParA gro...
  10. Role of MinD-membrane association in Min protein interactions.

    Journal of Bacteriology 188(8):2993 (2006) PMID 16585760 PMCID PMC1446990

    Division site placement in Escherichia coli involves interactions of the MinD protein with MinC and MinE and with other MinD molecules to form membrane-associated polymeric structures. In this work, as part of a study of these interactions, we established that heterologous membrane-associated pr...
  11. Spatial control of bacterial division-site placement.

    Nature Reviews: Microbiology 3(12):959 (2005) PMID 16322744

    The site of cell division in bacterial cells is placed with high fidelity at a designated position, usually the midpoint of the cell. In normal cell division in Escherichia coli this is accomplished by the action of the Min proteins, which maintain a high concentration of a septation inhibitor n...
  12. The MreB and Min cytoskeletal-like systems play independent roles in prokaryotic polar differentiation.

    Molecular Microbiology 58(4):917 (2005) PMID 16262780

    Establishment of an axis of cell polarity and differentiation of the cell poles are fundamental aspects of cellular development in many organisms. We compared the effects of two bacterial cytoskeletal-like systems, the MreB and MinCDE systems, on these processes in Escherichia coli. We report th...
  13. Positioning of the MinE binding site on the MinD surface suggests a plausible mechanism for activation of the Escherichia coli MinD ATPase during division site selection.

    Molecular Microbiology 54(1):99 (2004) PMID 15458408

    Division site selection in Escherichia coli requires that the MinD protein interact with itself and with MinC and MinE. MinD is a member of the NifH-ArsA-Par-MinD subgroup of ATPases. The MinE-MinD interaction results in activation of MinD ATPase activity in the presence of membrane vesicles. Th...
  14. Mapping the MinE site involved in interaction with the MinD division site selection protein of Escherichia coli.

    Journal of Bacteriology 185(16):4948 (2003) PMID 12897015 PMCID PMC166455

    Interactions between the MinD and MinE proteins are required for proper placement of the Escherichia coli division septum. The site within MinE that is required for interaction with MinD was mapped by studying the effects of site-directed minE mutations on MinD-MinE interactions in yeast two-hyb...
  15. Division site selection in Escherichia coli involves dynamic redistribution of Min proteins within coiled structures that extend between the two cell poles.

    PNAS 100(13):7865 (2003) PMID 12766229 PMCID PMC164679

    The MinCDE proteins of Escherichia coli are required for proper placement of the division septum at midcell. The site selection process requires the rapid oscillatory redistribution of the proteins from pole to pole. We report that the three Min proteins are organized into extended membrane-asso...
  16. New insights into the developmental history of the bacterial cell division site.

    Journal of Bacteriology 185(4):1125 (2003) PMID 12562780 PMCID PMC142895

  17. Division site placement in E.coli: mutations that prevent formation of the MinE ring lead to loss of the normal midcell arrest of growth of polar MinD membrane domains.

    EMBO Journal 21(13):3347 (2002) PMID 12093736 PMCID PMC126078

    The MinE protein functions as a topological specificity factor in determining the site of septal placement in Escherichia coli. MinE assembles into a membrane-associated ring structure near midcell and directs the localization of MinD and MinC into a membrane- associated polar zone that undergoe...
  18. Analysis of the length distribution of murein glycan strands inftsZandftsImutants ofE. coli

    FEMS Microbiology Letters 168(1):71 (1998)

    The chain length distribution of murein glycan strands was analyzed in wild-type cells and in cells in which preseptal and/or septal murein synthesis was prevented in ftsZ84 and ftsI36 mutants of E. coli. This revealed a significant change in glycan chain lengths in new...
  19. [41] Reconstitution of lipopolysaccharide-phospholipid-transferase enzyme complexes of bacterial cell envelopes

    Methods in Enzymology 32:449 (1974)

    A series of membrane-bound enzymes in Salmonella typhimurium and Escherichia coli catalyzes the sequential transfer of glycosyl residues from nucleotide sugar precursors to the lipopolysaccharide of these organisms. Glucose-deficient LPS is isolated from mutant strains of S. typhimuriu...
  20. 1 - BIOLOGICAL MEMBRANES: AN OVERVIEW AT THE MOLECULAR LEVEL

    This chapter provides an overview of biological membranes at the molecular level. Biological membranes are continuous structures separating two aqueous phases. They are relatively impermeable to water-soluble compounds, show a characteristic trilaminar appearance when fixed sections are ...