An Expression System of Rat Calmodulin Using T7 Phage Promoter inEscherichia coli

1998 ◽  
Vol 12 (1) ◽  
pp. 25-28 ◽  
Author(s):  
Nobuhiro Hayashi ◽  
Mamoru Matsubara ◽  
Akihiko Takasaki ◽  
Koiti Titani ◽  
Hisaaki Taniguchi
Keyword(s):  
Expression System ◽  
Inescherichia Coli ◽  
T7 Phage

scholarly journals T7 phage factor required for managing RpoS inEscherichia coli

2018 ◽  
Vol 115 (23) ◽  
pp. E5353-E5362 ◽  
Author(s):  
Aline Tabib-Salazar ◽  
Bing Liu ◽  
Declan Barker ◽  
Lynn Burchell ◽  
Udi Qimron ◽  
...  
Keyword(s):  
Stationary Phase ◽  
Stationary Phases ◽  
Inescherichia Coli ◽  
E Coli ◽  
Bacterial Transcription ◽  
Bacterial Rna ◽  
Predominant Form ◽  
Phage Development ◽  
T7 Phage

T7 development inEscherichia colirequires the inhibition of the housekeeping form of the bacterial RNA polymerase (RNAP), Eσ70, by two T7 proteins: Gp2 and Gp5.7. Although the biological role of Gp2 is well understood, that of Gp5.7 remains to be fully deciphered. Here, we present results from functional and structural analyses to reveal that Gp5.7 primarily serves to inhibit EσS, the predominant form of the RNAP in the stationary phase of growth, which accumulates in exponentially growingE. colias a consequence of the buildup of guanosine pentaphosphate [(p)ppGpp] during T7 development. We further demonstrate a requirement of Gp5.7 for T7 development inE. colicells in the stationary phase of growth. Our finding represents a paradigm for how some lytic phages have evolved distinct mechanisms to inhibit the bacterial transcription machinery to facilitate phage development in bacteria in the exponential and stationary phases of growth.

Expression of Pseudomonas amyloderamosa isoamylase gene in Escherichia coli using an inducible T7 phage expression system

1995 ◽  
Vol 30 (6) ◽  
pp. 547-552 ◽  
Author(s):  
Long-Liu Lin ◽  
Wen-Shen Chu
Keyword(s):  
Escherichia Coli ◽  
Expression System ◽  
T7 Phage

Stability studies with different vector backbones utilizing the T7 expression system inEscherichia coli

2008 ◽  
Vol 83 (8) ◽  
pp. 1120-1125 ◽  
Author(s):  
Rupali Walia ◽  
Jahar Kanti Deb ◽  
Krishna Jyoti Mukherjee
Keyword(s):  
Expression System ◽  
Inescherichia Coli ◽  
Stability Studies ◽  
T7 Expression System

Establishment of a low-dosage-IPTG inducible expression system construction method inEscherichia coli

2018 ◽  
Vol 58 (9) ◽  
pp. 806-810 ◽  
Author(s):  
Ming Zhao ◽  
Xin-Yi Tao ◽  
Feng-Qing Wang ◽  
Yu-Hong Ren ◽  
Dong-Zhi Wei
Keyword(s):  
Expression System ◽  
Inducible Expression ◽  
Construction Method ◽  
Inescherichia Coli ◽  
System Construction ◽  
Inducible Expression System ◽  
Low Dosage

Electron Microscopy of Bacteriophage T7 Internal Head Proteins

1975 ◽  
Vol 33 ◽  
pp. 638-639
Author(s):  
P. Serwer
Keyword(s):  
Electron Microscopy ◽  
Bacteriophage T7 ◽  
Specimen Preparation ◽  
Dna Molecule ◽  
The Core ◽  
Internal Core ◽  
Phage T7 ◽  
T7 Phage ◽  
Preparation Techniques ◽  
Internal Head

The genome of bacteriophage T7 is a duplex DNA molecule packaged in a space whose volume has been measured to be 2.2 x the volume of the B form of T7 DNA. To help determine the mechanism for packaging this DNA, the configuration of proteins inside the phage head has been investigated by electron microscopy. A core which is roughly cylindrical in outline has been observed inside the head of phage T7 using three different specimen preparation techniques.When T7 phage are treated with glutaraldehyde, DNA is ejected from the head often revealing an internal core (dark arrows in Fig. 1). When both the core and tail are present in a particle, the core appears to be coaxial with the tail. Core-tail complexes sometimes dislodge from their normal location and appear attached to the outside of a phage head (light arrow in Fig. 1).

High Level Expression of Active Human Prothrombin in a Vaccina Virus Expression System

1992 ◽  
Vol 68 (02) ◽  
pp. 119-124 ◽  
Author(s):  
F G Falkner ◽  
P L Turecek ◽  
R T A MacGillivray ◽  
W Bodemer ◽  
F Scheiflinger ◽  
...  
Keyword(s):  
Vaccinia Virus ◽  
Cell Lines ◽  
Expression System ◽  
Human Cell Line ◽  
Cell System ◽  
Time Saving ◽  
Expression Levels ◽  
Mammalian Cell Lines ◽  
Cell Line Hela ◽  
Virus Expression

SummaryWe have worked out an efficient and time saving procedure for the expression of recombinant human prothrombin. The glycoprotein was expressed in the vaccinia virus expression system in several mammalian cell lines. The kidney cell lines Vero and BHK and the human cell line Hela were found to efficiently secrete prothrombin. Expression levels of 3–4 µg of factor II per 106 cells per day corresponding to 18–23 mU per 106 cells per day were achieved. Since the expression levels obtained with the vaccinia virus/Vero cell system were comparable to those obtained in amplified transformed CHO cells it provides an alternative system for the efficient expression of human prothrombin and may allow to further elucidate structure-function relationships of (pro)thrombin and its various effectors.

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