Simultaneous utilization of glucose, xylose and arabinose in the presence of acetate by a consortium of Escherichia coli strains

Bacteria are known to consume some sugars over others, although recent work reported by Koirala and colleagues in this issue of theJournal of Bacteriology(S. Koirala, X. Wang, and C. V. Rao, J Bacteriol 198:386–393, 2016,http://dx.doi.org/10.1128/JB.00709-15) revealed that individual cells do not necessarily follow this hierarchy. By studying the preferential consumption ofl-arabinose overd-xylose inEscherichia coli, those authors found that subpopulations consume one, the other, or both sugars through cross-repression between utilization pathways. Their findings challenge classic assertions about established hierarchies and can guide efforts to engineer the simultaneous utilization of multiple sugars.

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Efficient succinic acid production from lignocellulosic biomass by simultaneous utilization of glucose and xylose in engineered Escherichia coli

Bioresource Technology ◽

10.1016/j.biortech.2013.09.052 ◽

2013 ◽

Vol 149 ◽

pp. 84-91 ◽

Cited By ~ 49

Author(s):

Rongming Liu ◽

Liya Liang ◽

Feng Li ◽

Mingke Wu ◽

Kequan Chen ◽

...

Keyword(s):

Escherichia Coli ◽

Succinic Acid ◽

Lignocellulosic Biomass ◽

Acid Production ◽

Simultaneous Utilization ◽

Succinic Acid Production ◽

Engineered Escherichia Coli

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Regulation underlying hierarchical and simultaneous utilization of carbon substrates by flux sensors in Escherichia coli

Nature Microbiology ◽

10.1038/s41564-019-0610-7 ◽

2019 ◽

Vol 5 (1) ◽

pp. 206-215 ◽

Cited By ~ 5

Author(s):

Hiroyuki Okano ◽

Rutger Hermsen ◽

Karl Kochanowski ◽

Terence Hwa

Keyword(s):

Escherichia Coli ◽

Simultaneous Utilization ◽

Carbon Substrates

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

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100081693 ◽

1978 ◽

Vol 36 (2) ◽

pp. 166-167 ◽

Cited By ~ 1

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).

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

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100060490 ◽

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.

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