Structural and functional studies on a mesophilic stationary phase survival protein (Sur E) from Salmonella typhimurium

FEBS Journal ◽  
2008 ◽  
Vol 275 (23) ◽  
pp. 5855-5864 ◽  
Author(s):  
A. Pappachan ◽  
H. S. Savithri ◽  
M. R. N. Murthy
Keyword(s):  
Stationary Phase ◽  
Salmonella Typhimurium ◽  
Functional Studies ◽  
Stationary Phase Survival

Growth potential of exponential- and stationary-phase Salmonella Typhimurium during sausage fermentation

Meat Science ◽  
2016 ◽  
Vol 121 ◽  
pp. 342-349 ◽  
Author(s):  
T. Birk ◽  
S. Henriksen ◽  
K. Müller ◽  
T.B. Hansen ◽  
S. Aabo
Keyword(s):  
Stationary Phase ◽  
Salmonella Typhimurium ◽  
Growth Potential

scholarly journals Novobiocin Sensitivity of Salmonella typhimurium dam and/or seqA Mutants

2014 ◽  
Vol 63 (1) ◽  
pp. 51-56 ◽  
Author(s):  
ABDELWAHEB CHATTI ◽  
MERIEM ALOUI ◽  
JIHEN TAGOURTI ◽  
MOUADH MIHOUB ◽  
AHMED LANDOULSI
Keyword(s):  
Dna Methylation ◽  
Stationary Phase ◽  
Salmonella Typhimurium ◽  
The Other ◽  
Protein Profiles ◽  
Wild Type ◽  
Whole Cell ◽  
Expression Levels

This study was carried out to determine the effects of novobiocin, a gyrase inhibitor, on the growth, survival, motility and whole cell proteins of S. Typhimurium dam and/or seqA strains. Our results showed that the dam and seqA/dam mutants are the most sensitive to novobiocin, compared to wild type and seqA strains. Surprisingly, the motility of seqA mutants increased after exposure to novobiocin only in stationary phase cells. All the other strains showed a significant decrease in their motility. The analysis of protein profiles of all strains demonstrated several modifications as manifested by the alteration of the expression levels of certain bands. Our work is therefore of great interest in understanding the effects of novobiocin on S. Typhimurium and the involvement of DNA methylation.

scholarly journals Extracytoplasmic Function σ Factors Regulate Expression of the Bacillus subtilis yabE Gene via a cis-Acting Antisense RNA

2008 ◽  
Vol 191 (3) ◽  
pp. 1101-1105 ◽  
Author(s):  
Warawan Eiamphungporn ◽  
John D. Helmann
Keyword(s):  
Bacillus Subtilis ◽  
Stationary Phase ◽  
Antisense Rna ◽  
Cis Acting ◽  
Stationary Phase Survival

ABSTRACT Bacillus subtilis yabE encodes a predicted resuscitation-promoting factor/stationary-phase survival (Rpf/Sps) family autolysin. Here, we demonstrate that yabE is negatively regulated by a cis-acting antisense RNA which, in turn, is regulated by two extracytoplasmic function σ factors: σX and σM.

scholarly journals Structural and functional studies on Salmonella typhimurium pyridoxal kinase: the first structural evidence for the formation of Schiff base with the substrate

FEBS Journal ◽  
2019 ◽  
Vol 286 (18) ◽  
pp. 3684-3700 ◽  
Author(s):  
Geeta Deka ◽  
Josyula N. Kalyani ◽  
Fathima Benazir Jahangir ◽  
Pallavi Sabharwal ◽  
Handanahal S. Savithri ◽  
...  
Keyword(s):  
Schiff Base ◽  
Salmonella Typhimurium ◽  
Pyridoxal Kinase ◽  
Functional Studies

scholarly journals Structural and functional insights into the stationary-phase survival protein SurE, an important virulence factor ofBrucella abortus

2016 ◽  
Vol 72 (5) ◽  
pp. 386-396
Author(s):  
K. F. Tarique ◽  
S. A. Abdul Rehman ◽  
S. Devi ◽  
Priya Tomar ◽  
S. Gourinath
Keyword(s):  
Crystal Structure ◽  
Stationary Phase ◽  
Brucella Abortus ◽  
Active Site ◽  
Drug Target ◽  
Oligomeric State ◽  
Common Features ◽  
Terminal Domain ◽  
Important Virulence Factor ◽  
Stationary Phase Survival

The stationary-phase survival protein SurE fromBrucella abortus(BaSurE) is a metal-dependent phosphatase that is essential for the survival of this bacterium in the stationary phase of its life cycle. Here, BaSurE has been biochemically characterized and its crystal structure has been determined to a resolution of 1.9 Å. BaSurE was found to be a robust enzyme, showing activity over wide ranges of temperature and pH and with various phosphoester substrates. The active biomolecule is a tetramer and each monomer was found to consist of two domains: an N-terminal domain, which forms an approximate α + β fold, and a C-terminal domain that belongs to the α/β class. The active site lies at the junction of these two domains and was identified by the presence of conserved negatively charged residues and a bound Mg2+ion. Comparisons of BaSurE with its homologues have revealed both common features and differences in this class of enzymes. The number and arrangement of some of the equivalent secondary structures, which are seen to differ between BaSurE and its homologues, are responsible for a difference in the size of the active-site area and the overall oligomeric state of this enzyme in other organisms. As it is absent in mammals, it has the potential to be a drug target.

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