Non-random segregation of sister chromosomes in Escherichia coli

Nature ◽  
2008 ◽  
Vol 455 (7217) ◽  
pp. 1248-1250 ◽  
Author(s):  
Martin A. White ◽  
John K. Eykelenboom ◽  
Manuel A. Lopez-Vernaza ◽  
Emily Wilson ◽  
David R. F. Leach
Keyword(s):  
Escherichia Coli ◽  
Random Segregation

scholarly journals Non-random segregation of sister chromosomes by Escherichia coli MukBEF axial cores

2020 ◽  
Author(s):  
Jarno Mäkelä ◽  
Stephan Uphoff ◽  
David J. Sherratt
Keyword(s):  
Escherichia Coli ◽  
Genetic Material ◽  
Temporal Organization ◽  
Translational Symmetry ◽  
Cell Axis ◽  
Chromosome Conformation ◽  
Random Segregation ◽  
Spatio Temporal ◽  
Replication Terminus ◽  
Dna Strand

SummaryThe Escherichia coli structural maintenance of chromosomes complex, MukBEF, forms axial cores to chromosomes that determine their spatio-temporal organization. Here, we show that axial cores direct chromosome arms to opposite poles and generate the translational symmetry between newly replicated sister chromosomes. MatP, a replication terminus (ter) binding protein prevents chromosome rotation around the longitudinal cell axis by displacing MukBEF from ter, thereby maintaining the linear shape of axial cores. During DNA replication, MukBEF action directs lagging strands towards the cell center, marked by accumulation of DNA-bound β2-clamps in the wake of replisomes, in a process necessary for the translational symmetry of sister chromosomes. Finally, the ancestral (‘immortal’) template DNA strand, propagated from previous generations, is preferentially inherited by the cell forming at the old pole, dependent on MukBEF-MatP. The work demonstrates how chromosome organization-segregation can foster non-random inheritance of genetic material and provides a framework for understanding how chromosome conformation and dynamics shape subcellular organization.

Non-random segregation of DNA strands in Escherichia coli

1973 ◽  
Vol 80 (3) ◽  
pp. 477-503 ◽  
Author(s):  
O. Pierucci ◽  
C. Zuchowski
Keyword(s):  
Escherichia Coli ◽  
Dna Strands ◽  
Random Segregation

Escherichia coli minichromosomes: Random segregation and absence of copy number control

1990 ◽  
Vol 215 (2) ◽  
pp. 257-265 ◽  
Author(s):  
Martin Roland Jensen ◽  
Anders Løbner-Olesen ◽  
Knud V. Rasmussen
Keyword(s):  
Escherichia Coli ◽  
Copy Number ◽  
Copy Number Control ◽  
Random Segregation

Structural organization of escherichia coli ribosomes as determined by immuno electron microscopy

1978 ◽  
Vol 36 (2) ◽  
pp. 166-167 ◽  
Author(s):  
G. Stöffler ◽  
R.W. Bald ◽  
J. Dieckhoff ◽  
H. Eckhard ◽  
R. Lührmann ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Escherichia Coli ◽  
Ribosomal Proteins ◽  
Structural Organization ◽  
Three Dimensional ◽  
Ribosomal Subunit ◽  
Spatial Arrangement ◽  
Small Subunit ◽  
Antibody Binding ◽  
Immuno Electron Microscopy

A central step towards an understanding of the structure and function of the Escherichia coli ribosome, a large multicomponent assembly, is the elucidation of the spatial arrangement of its 54 proteins and its three rRNA molecules. The structural organization of ribosomal components has been investigated by a number of experimental approaches. Specific antibodies directed against each of the 54 ribosomal proteins of Escherichia coli have been performed to examine antibody-subunit complexes by electron microscopy. The position of the bound antibody, specific for a particular protein, can be determined; it indicates the location of the corresponding protein on the ribosomal surface.The three-dimensional distribution of each of the 21 small subunit proteins on the ribosomal surface has been determined by immuno electron microscopy: the 21 proteins have been found exposed with altogether 43 antibody binding sites. Each one of 12 proteins showed antibody binding at remote positions on the subunit surface, indicating highly extended conformations of the proteins concerned within the 30S ribosomal subunit; the remaining proteins are, however, not necessarily globular in shape (Fig. 1).

Sites of Adsorption of the Bacteriophages T3 and T5 on the Wall of Escherichia Coli B.

1967 ◽  
Vol 25 ◽  
pp. 96-97
Author(s):  
Manfred E. Bayer
Keyword(s):  
Escherichia Coli ◽  
Cell Wall ◽  
Electron Microscope ◽  
Uranyl Acetate ◽  
E Coli ◽  
Receptor Sites ◽  
Rigid Cell Wall ◽  
Host Cell Surface ◽  
Bacterial Viruses ◽  
Escherichia Coli B

Bacterial viruses adsorb specifically to receptors on the host cell surface. Although the chemical composition of some of the cell wall receptors for bacteriophages of the T-series has been described and the number of receptor sites has been estimated to be 150 to 300 per E. coli cell, the localization of the sites on the bacterial wall has been unknown.When logarithmically growing cells of E. coli are transferred into a medium containing 20% sucrose, the cells plasmolize: the protoplast shrinks and becomes separated from the somewhat rigid cell wall. When these cells are fixed in 8% Formaldehyde, post-fixed in OsO4/uranyl acetate, embedded in Vestopal W, then cut in an ultramicrotome and observed with the electron microscope, the separation of protoplast and wall becomes clearly visible, (Fig. 1, 2). At a number of locations however, the protoplasmic membrane adheres to the wall even under the considerable pull of the shrinking protoplast. Thus numerous connecting bridges are maintained between protoplast and cell wall. Estimations of the total number of such wall/membrane associations yield a number of about 300 per cell.

Infection of Escherichia coli with bacteriophages

1969 ◽  
Vol 27 ◽  
pp. 370-371
Author(s):  
Manfred E. Bayer
Keyword(s):  
Escherichia Coli ◽  
Nucleic Acid ◽  
Cell Surface ◽  
Virus Type ◽  
Infection Process ◽  
Adsorption Site ◽  
The Other ◽  
Specific Receptors ◽  
Bacterial Receptors

The first step in the infection of a bacterium by a virus consists of a collision between cell and bacteriophage. The presence of virus-specific receptors on the cell surface will trigger a number of events leading eventually to release of the phage nucleic acid. The execution of the various "steps" in the infection process varies from one virus-type to the other, depending on the anatomy of the virus. Small viruses like ØX 174 and MS2 adsorb directly with their capsid to the bacterial receptors, while other phages possess attachment organelles of varying complexity. In bacteriophages T3 (Fig. 1) and T7 the small conical processes of their heads point toward the adsorption site; a welldefined baseplate is attached to the head of P22; heads without baseplates are not infective.

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