A modified uridine in the first position of the anticodon of a minor species of arginine tRNA, the argU gene product, from Escherichia coli

1993 ◽  
Vol 216 (2) ◽  
pp. 369-375 ◽  
Author(s):  
Kensaku SAKAMOTO ◽  
Gota KAWAI ◽  
Tatsuya NIIMI ◽  
Takahiko SATOH ◽  
Mitsuo SEKINE ◽  
...  
2000 ◽  
Vol 182 (20) ◽  
pp. 5779-5786 ◽  
Author(s):  
Stéphanie Gon ◽  
Jean-Claude Patte ◽  
Vincent Méjean ◽  
Chantal Iobbi-Nivol

ABSTRACT The bisZ gene of Escherichia coli was previously described as encoding a minor biotin sulfoxide (BSO) reductase in addition to the main cytoplasmic BSO reductase, BisC. In this study, bisZ has been renamed torZ based on the findings that (i) the torZ gene product, TorZ, is able to reduce trimethylamine N-oxide (TMAO) more efficiently than BSO; (ii) although TorZ is more homologous to BisC than to the TMAO reductase TorA (63 and 42% identity, respectively), it is located mainly in the periplasm as is TorA; (iii)torZ belongs to the torYZ operon, and the first gene, torY (formerly yecK), encodes a pentahemic c-type cytochrome homologous to the TorC cytochrome of the TorCAD respiratory system. Furthermore, the torYZ operon encodes a third TMAO respiratory system, with catalytic properties that are clearly different from those of the TorCAD and the DmsABC systems. ThetorYZ and the torCAD operons may have diverged from a common ancestor, but, surprisingly, notorD homologue is found in the sequences aroundtorYZ. Moreover, the torYZ operon is expressed at very low levels under the conditions tested, and, in contrast to torCAD, it is not induced by TMAO or dimethyl sulfoxide.


1993 ◽  
Vol 268 (35) ◽  
pp. 26041-26044
Author(s):  
K Saiki ◽  
T Mogi ◽  
K Ogura ◽  
Y Anraku

1987 ◽  
Vol 248 (1) ◽  
pp. 43-51 ◽  
Author(s):  
J Charlier ◽  
R Sanchez

In contrast with most aminoacyl-tRNA synthetases, the lysyl-tRNA synthetase of Escherichia coli is coded for by two genes, the normal lysS gene and the inducible lysU gene. During its purification from E. coli K12, lysyl-tRNA synthetase was monitored by its aminoacylation and adenosine(5′)tetraphospho(5′)adenosine (Ap4A) synthesis activities. Ap4A synthesis was measured by a new assay using DEAE-cellulose filters. The heterogeneity of lysyl-tRNA synthetase (LysRS) was revealed on hydroxyapatite; we focused on the first peak, LysRS1, because of its higher Ap4A/lysyl-tRNA activity ratio at that stage. Additional differences between LysRS1 and LysRS2 (major peak on hydroxyapatite) were collected. LysRS1 was eluted from phosphocellulose in the presence of the substrates, whereas LysRS2 was not. Phosphocellulose chromatography was used to show the increase of LysRS1 in cells submitted to heat shock. Also, the Mg2+ optimum in the Ap4A-synthesis reaction is much higher for LysRS1. LysRS1 showed a higher thermostability, which was specifically enhanced by Zn2+. These results in vivo and in vitro strongly suggest that LysRS1 is the heat-inducible lysU-gene product.


Microbiology ◽  
1985 ◽  
Vol 131 (2) ◽  
pp. 239-244
Author(s):  
A. TORMO ◽  
C. FERNANDEZ-CABRERA ◽  
M. VICENTE

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