scholarly journals The umpA gene of Escherichia coli encodes phosphatidylglycerol:prolipoprotein diacylglyceryl transferase (lgt) and regulates thymidylate synthase levels through translational coupling.

1995 ◽  
Vol 177 (7) ◽  
pp. 1879-1882 ◽  
Author(s):  
K Gan ◽  
K Sankaran ◽  
M G Williams ◽  
M Aldea ◽  
K E Rudd ◽  
...  
1989 ◽  
Vol 264 (32) ◽  
pp. 19132-19137
Author(s):  
I K Dev ◽  
B B Yates ◽  
J Atashi ◽  
W S Dallas

1989 ◽  
Vol 264 (16) ◽  
pp. 9145-9148 ◽  
Author(s):  
V J Davisson ◽  
W Sirawaraporn ◽  
D V Santi

2008 ◽  
Vol 40 (10) ◽  
pp. 2206-2217 ◽  
Author(s):  
Aldo A. Arvizu-Flores ◽  
Rocio Sugich-Miranda ◽  
Rodrigo Arreola ◽  
Karina D. Garcia-Orozco ◽  
Enrique F. Velazquez-Contreras ◽  
...  

1993 ◽  
Vol 39 (4) ◽  
pp. 448-450 ◽  
Author(s):  
E. Tiganos ◽  
M. B. Herrington

Thymine-requiring strains of Escherichia coli suppress nonsense and frame-shift mutations. This appears to occur during translation, suggesting that the lack of activity of an enzyme thymidylate synthase, required for the synthesis of a DNA precursor, alters the fidelity of translation. The aminoglycoside antibiotic kasugamycin, which enhances translational accuracy in vitro, prevents thymine-requiring cells from suppressing. The inhibition of suppression by kasugamycin is not prevented by the introduction of two different kasugamycin-resistance mutations, although the dose required for inhibition increases. These observations support the conclusion that suppression occurs during translation.Key words: suppression, kasugamycin, translation, thymine-requiring.


1998 ◽  
Vol 180 (19) ◽  
pp. 5240-5242 ◽  
Author(s):  
Donald Oliver ◽  
Jessica Norman ◽  
Shameema Sarker

ABSTRACT secA is translationally regulated by the protein secretion proficiency state of the Escherichia coli cell. This regulation was explored by making signal sequence mutations in the gene upstream of secA, gene X, which promotessecA translational coupling. Gene X signal sequence mutants were constitutive for secA expression, whileprlA alleles partially restored secAregulation. These results show that interaction of the pre-gene X protein with the translocon is required for proper secAregulation. Furthermore, gene X signal sequence mutations disruptedsecA regulation only in the cis configuration. We propose that nascent pre-gene X protein interacts with the translocon during its secretion to constitute the secretion sensor.


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