Developing an Extended Genomic Engineering Approach Based on Recombineering to Knock-in Heterologous Genes to Escherichia coli Genome

2011 ◽  
Vol 51 (2) ◽  
pp. 109-118 ◽  
Author(s):  
Karan Sukhija ◽  
Michael Pyne ◽  
Saad Ali ◽  
Valerie Orr ◽  
Daryoush Abedi ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Genomic Engineering ◽  
Engineering Approach

scholarly journals Secretion of polyhydroxybutyrate in Escherichia coli using a synthetic biological engineering approach

2013 ◽  
Vol 7 (1) ◽  
pp. 24 ◽  
Author(s):  
Asif Rahman ◽  
Elisabeth Linton ◽  
Alex D Hatch ◽  
Ronald C Sims ◽  
Charles D Miller
Keyword(s):  
Escherichia Coli ◽  
Biological Engineering ◽  
Engineering Approach

Genomic engineering of Escherichia coli for production of intermediate metabolites in the aromatic pathway

2011 ◽  
Vol 42 (1) ◽  
pp. 34-40 ◽  
Author(s):  
Po Ting Chen ◽  
Chung-Jen Chiang ◽  
Jen-You Wang ◽  
Ming-Zei Lee ◽  
Yun-Peng Chao
Keyword(s):  
Escherichia Coli ◽  
Genomic Engineering ◽  
Intermediate Metabolites ◽  
Aromatic Pathway

scholarly journals The discovery and development of the CRISPR system in applications in genome manipulation

2017 ◽  
Vol 95 (2) ◽  
pp. 203-210 ◽  
Author(s):  
Veronica Lau ◽  
James R. Davie
Keyword(s):  
Escherichia Coli ◽  
Immune System ◽  
Adaptive Immune System ◽  
Genomic Engineering ◽  
Adaptive Immune ◽  
Crispr System ◽  
Genome Regulation ◽  
Short Palindromic Repeat ◽  
The Moment ◽  
Genome Manipulation

The clustered regularly interspaced short palindromic repeat (CRISPR) associated 9 (Cas9) system is a microbial adaptive immune system that has been recently developed for genomic engineering. From the moment the CRISPR system was discovered in Escherichia coli, the drive to understand the mechanism prevailed, leading to rapid advancement in the knowledge and applications of the CRISPR system. With the ability to characterize and understand the function of the Cas9 endonuclease came the ability to adapt the CRISPR–Cas9 system for use in a variety of applications and disciplines ranging from agriculture to biomedicine. This review will provide a brief overview of the discovery and development of the CRISPR–Cas9 system in applications such as genome regulation and epigenome engineering, as well as the challenges faced.

Genomic engineering of Escherichia coli by the phage attachment site-based integration system with mutant loxP sites

2012 ◽  
Vol 47 (12) ◽  
pp. 2246-2254 ◽  
Author(s):  
Chung-Jen Chiang ◽  
Mukesh Saini ◽  
Hong Min Lee ◽  
Zei Wen Wang ◽  
Li-Jen Lin ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Attachment Site ◽  
Integration System ◽  
Genomic Engineering

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.

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