Melibiose permease and .alpha.-galactosidase of Escherichia coli: identification by selective labeling using a T7 RNA polymerase/promoter expression system

Biochemistry ◽  
1990 ◽  
Vol 29 (3) ◽  
pp. 690-696 ◽  
Author(s):  
Thierry Pourcher ◽  
Martine Bassilana ◽  
Hemanta K. Sarkar ◽  
H. Ronald Kaback ◽  
Gerard Leblanc
Gene ◽  
1994 ◽  
Vol 142 (1) ◽  
pp. 61-66 ◽  
Author(s):  
Marina I. Lebedeva ◽  
Ekaterina V. Rogozhkina ◽  
Nikolay A. Tsyba ◽  
Sergey V. Mashko

2021 ◽  
Author(s):  
Christopher Deich ◽  
Brock Cash ◽  
Wakana Sato ◽  
Judee Sharon ◽  
Lauren Aufdembrink ◽  
...  

Efficient cell-free protein expression from linear DNA templates has remained a challenge primarily due to template degradation. Here we present a modified T7 RNA polymerase promoter that acts to significantly increase the yields of both transcription and translation within in vitro systems. The modified promoter, termed T7Max, recruits standard T7 RNA polymerase, so no protein engineering is needed to take advantage of this method. This technique could be used with any T7 RNA polymerase- based in vitro protein expression system. Unlike other methods of limiting linear template degradation, the T7Max promoter increases transcript concentration in a T7 transcription reaction, providing more mRNA for translation.


2003 ◽  
Vol 19 (4) ◽  
pp. 367-373 ◽  
Author(s):  
I. Yu. Slavchenko ◽  
E. V. Boreyko ◽  
N. V. Vorobey ◽  
S. I. Chernykh ◽  
V. A. Kordyum

2013 ◽  
Vol 97 (17) ◽  
pp. 7755-7766 ◽  
Author(s):  
Md. Javed Equbal ◽  
Preeti Srivastava ◽  
Gopal Prasad Agarwal ◽  
Jahar Kanti Deb

1987 ◽  
Vol 262 (9) ◽  
pp. 3940-3943
Author(s):  
M. Yamagishi ◽  
J.R. Cole ◽  
M. Nomura ◽  
F.W. Studier ◽  
J.J. Dunn

Biochemistry ◽  
1995 ◽  
Vol 34 (2) ◽  
pp. 666-672 ◽  
Author(s):  
Charlie Schick ◽  
Craig T. Martin

1993 ◽  
Vol 15 (8) ◽  
Author(s):  
Norihiro Nishimura ◽  
Yoshihisa Kitaoka ◽  
Akio Mimura ◽  
Yoshimasa Takahara

2005 ◽  
Vol 33 (1) ◽  
pp. 56-58 ◽  
Author(s):  
T. Drepper ◽  
S. Arvani ◽  
F. Rosenau ◽  
S. Wilhelm ◽  
K.-E. Jaeger

High-level synthesis of complex enzymes like bacterial [NiFe] hydrogenases, in general, requires an expression system that allows concerted expression of a large number of genes. So far, it has not been possible to overproduce a hydrogenase in a stable and active form by using a customary expression system. Therefore we started to establish a new, T7-based expression system in the phototrophic bacterium Rhodobacter capsulatus. The beneficial properties of this bacterial host in combination with the unique capacity of T7 RNA polymerase to synthesize long transcripts will allow the high-level synthesis and assembly of active hydrogenase as well as other complex enzymes in the near future.


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