Genetic manipulation of the restricted facultative methylotroph Hyphomicrobium X by the R-plasmid-mediated introduction of the Escherichia coli pdh genes

1984 ◽  
Vol 139 (4) ◽  
pp. 311-318 ◽  
Author(s):  
L. Dijkhuizen ◽  
W. Harder ◽  
L. de Boer ◽  
A. van Boven ◽  
W. Clement ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Genetic Manipulation ◽  
Facultative Methylotroph ◽  
Restricted Facultative Methylotroph

scholarly journals Alteration of the Phospholipid Composition of Escherichia coli through Genetic Manipulation

1989 ◽  
Vol 264 (25) ◽  
pp. 14972-14977
Author(s):  
P N Heacock ◽  
W Dowhan
Keyword(s):  
Escherichia Coli ◽  
Genetic Manipulation ◽  
Phospholipid Composition

Genetic manipulation of a primary metabolic pathway for l-ornithine production in Escherichia coli

2006 ◽  
Vol 28 (22) ◽  
pp. 1849-1856 ◽  
Author(s):  
Young-Joon Lee ◽  
Jae-Yong Cho
Keyword(s):  
Escherichia Coli ◽  
Metabolic Pathway ◽  
Genetic Manipulation

Genetic manipulation of Escherichia coli central carbon metabolism for efficient production of fumaric acid

2018 ◽  
Vol 270 ◽  
pp. 96-102 ◽  
Author(s):  
Huan Liu ◽  
Ruirui Song ◽  
Yue Liang ◽  
Ting Zhang ◽  
Li Deng ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Fumaric Acid ◽  
Carbon Metabolism ◽  
Genetic Manipulation ◽  
Central Carbon Metabolism ◽  
Efficient Production ◽  
Central Carbon

scholarly journals Engineering Escherichia coli to improve tryptophan production via genetic manipulation of precursor and cofactor pathways

2020 ◽  
Vol 5 (3) ◽  
pp. 200-205 ◽  
Author(s):  
Zhu Li ◽  
Dongqin Ding ◽  
Huiying Wang ◽  
Linxia Liu ◽  
Huan Fang ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Genetic Manipulation

Improved ethanol tolerance in Escherichia coli by changing the cellular fatty acids composition through genetic manipulation

2009 ◽  
Vol 31 (12) ◽  
pp. 1867-1871 ◽  
Author(s):  
Lian Hua Luo ◽  
Pil-Soo Seo ◽  
Jeong-Woo Seo ◽  
Sun-Yeon Heo ◽  
Dae-Hyuk Kim ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Fatty Acids ◽  
Ethanol Tolerance ◽  
Genetic Manipulation ◽  
Fatty Acids Composition ◽  
Cellular Fatty Acids

scholarly journals FtsN activates septal cell wall synthesis by forming a processive complex with the septum-specific peptidoglycan synthase in E. coli

2021 ◽  
Author(s):  
Zhixin Lyu ◽  
Atsushi Yahashiri ◽  
Xinxing Yang ◽  
Joshua W McCausland ◽  
Gabriela M Kaus ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Cell Wall ◽  
Single Molecule ◽  
Spatial Organization ◽  
Genetic Manipulation ◽  
Cell Wall Synthesis ◽  
Single Population ◽  
E Coli ◽  
Ftsz Ring ◽  
Synthesis Activity

The FtsN protein of Escherichia coli and other proteobacteria is an essential and highly conserved bitopic membrane protein that triggers the inward synthesis of septal peptidoglycan (sPG) during cell division. Previous work has shown that the activation of sPG synthesis by FtsN involves a series of interactions of FtsN with other divisome proteins and the cell wall. Precisely how FtsN achieves this role is unclear, but a recent study has shown that FtsN promotes the relocation of the essential sPG synthase FtsWI from an FtsZ-associated track (where FtsWI is inactive) to an sPG-track (where FtsWI engages in sPG synthesis). Whether FtsN works by displacing FtsWI from the Z-track or capturing/retaining FtsWI on the sPG-track is not known. Here we use single-molecule imaging and genetic manipulation to investigate the organization and dynamics of FtsN at the septum and how they are coupled to sPG synthesis activity. We found that FtsN exhibits a spatial organization and dynamics distinct from those of the FtsZ-ring. Single FtsN molecules move processively as a single population with a speed of ~ 9 nm s-1, similar to the speed of active FtsWI molecules on the sPG-track, but significantly different from the ~ 30 nm s-1 speed of inactive FtsWI molecules on the FtsZ-track. Furthermore, the processive movement of FtsN is independent of FtsZ's treadmilling dynamics but driven exclusively by active sPG synthesis. Importantly, only the essential domain of FtsN, a three-helix bundle in the periplasm, is required to maintain the processive complex containing both FtsWI and FtsN on the sPG-track. We conclude that FtsN activates sPG synthesis by forming a processive synthesis complex with FtsWI exclusively on the sPG-track. These findings favor a model in which FtsN captures or retains FtsWI on the sPG-track rather than one in which FtsN actively displaces FtsWI from the Z-track.

scholarly journals New approach to tryptophan production by Escherichia coli: genetic manipulation of composite plasmids in vitro.

1982 ◽  
Vol 43 (2) ◽  
pp. 289-297 ◽  
Author(s):  
S Aiba ◽  
H Tsunekawa ◽  
T Imanaka
Keyword(s):  
Escherichia Coli ◽  
Genetic Manipulation ◽  
New Approach

scholarly journals Profiling the Escherichia coli membrane protein interactome captured in Peptidisc libraries

eLife ◽  
2019 ◽  
Vol 8 ◽  
Author(s):  
Michael Luke Carlson ◽  
R Greg Stacey ◽  
John William Young ◽  
Irvinder Singh Wason ◽  
Zhiyu Zhao ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Membrane Protein ◽  
Protein Interactions ◽  
Genetic Manipulation ◽  
Protein Complexes ◽  
Cell Envelope ◽  
Protein Solubility ◽  
Rapid Identification ◽  
Bam Complex ◽  
Novel Approach

Protein-correlation-profiling (PCP), in combination with quantitative proteomics, has emerged as a high-throughput method for the rapid identification of dynamic protein complexes in native conditions. While PCP has been successfully applied to soluble proteomes, characterization of the membrane interactome has lagged, partly due to the necessary use of detergents to maintain protein solubility. Here, we apply the peptidisc, a ‘one-size fits all’ membrane mimetic, for the capture of the Escherichia coli cell envelope proteome and its high-resolution fractionation in the absence of detergent. Analysis of the SILAC-labeled peptidisc library via PCP allows generation of over 4900 possible binary interactions out of >700,000 random associations. Using well-characterized membrane protein systems such as the SecY translocon, the Bam complex and the MetNI transporter, we demonstrate that our dataset is a useful resource for identifying transient and surprisingly novel protein interactions. For example, we discover a trans-periplasmic supercomplex comprising subunits of the Bam and Sec machineries, including membrane-bound chaperones YfgM and PpiD. We identify RcsF and OmpA as bone fide interactors of BamA, and we show that MetQ association with the ABC transporter MetNI depends on its N-terminal lipid anchor. We also discover NlpA as a novel interactor of MetNI complex. Most of these interactions are largely undetected by standard detergent-based purification. Together, the peptidisc workflow applied to the proteomic field is emerging as a promising novel approach to characterize membrane protein interactions under native expression conditions and without genetic manipulation.

Sign in / Sign up

Export Citation Format

Share Document