Identification of the structural gene of the PEP-phosphotransferase enzyme I in Bacillus subtilis marburg

1975 ◽  
Vol 136 (4) ◽  
pp. 337-349 ◽  
Author(s):  
B. Niaudet ◽  
P. Gay ◽  
R. Dedonder
1983 ◽  
Vol 47 (1) ◽  
pp. 159-161 ◽  
Author(s):  
Yasutoshi TAKEICHI ◽  
Kazutaka OHMURA ◽  
Akira NAKAYAMA ◽  
Kiyotaka OTOZAI ◽  
Kunio YAMANE

1979 ◽  
Vol 43 (12) ◽  
pp. 2637-2638 ◽  
Author(s):  
S. NOMURA ◽  
K. YAMANE ◽  
T. MASUDA ◽  
F. KAWAMURA ◽  
T. MIZUKAMI ◽  
...  

1974 ◽  
Vol 128 (3) ◽  
pp. 213-221 ◽  
Author(s):  
J. -A. Lepesant ◽  
J. Lepesant-Kejzlarová ◽  
M. Pascal ◽  
F. Kunst ◽  
A. Billault ◽  
...  

2015 ◽  
Vol 25 (2-3) ◽  
pp. 94-105 ◽  
Author(s):  
Philippe Joyet ◽  
Meriem Derkaoui ◽  
Houda Bouraoui ◽  
Josef Deutscher

The hexitol <smlcap>D</smlcap>-mannitol is transported by many bacteria via a phosphoenolpyruvate (PEP):carbohydrate phosphotransferase system (PTS). In most Firmicutes, the transcription activator MtlR controls the expression of the genes encoding the <smlcap>D</smlcap>-mannitol-specific PTS components and <smlcap>D</smlcap>-mannitol-1-P dehydrogenase. MtlR contains an N-terminal helix-turn-helix motif followed by an Mga-like domain, two PTS regulation domains (PRDs), an EIIB<sup>Gat</sup>- and an EIIA<sup>Mtl</sup>-like domain. The four regulatory domains are the target of phosphorylation by PTS components. Despite strong sequence conservation, the mechanisms controlling the activity of MtlR from <i>Lactobacillus casei</i>, <i>Bacillus subtilis</i> and <i>Geobacillus stearothermophilus</i> are quite different. Owing to the presence of a tyrosine in place of the second conserved histidine (His) in PRD2, <i>L. casei</i> MtlR is not phosphorylated by Enzyme I (EI) and HPr. When the corresponding His in PRD2 of MtlR from <i>B. subtilis</i> and <i>G. stearothermophilus</i> was replaced with alanine, the transcription regulator was no longer phosphorylated and remained inactive. Surprisingly, <i>L. casei</i> MtlR functions without phosphorylation in PRD2 because in a <i>ptsI</i> (EI) mutant MtlR is constitutively active. EI inactivation prevents not only phosphorylation of HPr, but also of the PTS<sup>Mtl</sup> components, which inactivate MtlR by phosphorylating its EIIB<sup>Gat</sup>- or EIIA<sup>Mtl</sup>-like domain. This explains the constitutive phenotype of the <i>ptsI</i> mutant. The absence of EIIB<sup>Mtl</sup>-mediated phosphorylation leads to induction of the <i>L. casei</i><i>mtl </i>operon. This mechanism resembles <i>mtlARFD</i> induction in <i>G. stearothermophilus</i>, but differs from EIIA<sup>Mtl</sup>-mediated induction in <i>B. subtilis</i>. In contrast to <i>B. subtilis</i> MtlR, <i>L. casei</i> MtlR activation does not require sequestration to the membrane via the unphosphorylated EIIB<sup>Mtl</sup> domain.


Biochimie ◽  
1975 ◽  
Vol 56 (11-12) ◽  
pp. 1465-1470 ◽  
Author(s):  
J.A. Lepesant ◽  
A. Billault ◽  
J. Kejzlarová-Lepesant ◽  
M. Pascal ◽  
F. Kunst ◽  
...  

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