scholarly journals Molecular Basis of Stationary Phase Survival and Applications

2017 ◽  
Vol 8 ◽  
Author(s):  
Jananee Jaishankar ◽  
Preeti Srivastava
Keyword(s):  
Stationary Phase ◽  
Molecular Basis ◽  
Stationary Phase Survival

scholarly journals Pseudomonas-Saccharomyces Interactions: Influence of Fungal Metabolism on Bacterial Physiology and Survival

2005 ◽  
Vol 187 (3) ◽  
pp. 940-948 ◽  
Author(s):  
Julia D. Romano ◽  
Roberto Kolter
Keyword(s):  
Stationary Phase ◽  
Molecular Basis ◽  
Synthetic Medium ◽  
Grape Juice ◽  
Natural Environments ◽  
Bacterial Physiology ◽  
Beneficial Effects ◽  
Stationary Phase Survival ◽  
Yeast Mutants ◽  
Deletion Library

ABSTRACT Fungal-bacterial interactions are ubiquitous, yet their molecular basis is only poorly understood. In this study, a novel beneficial interaction between a strain of Pseudomonas putida and the fungus Saccharomyces cerevisiae was identified. When the bacteria were incubated alone in grape juice or in synthetic medium containing various concentrations of glucose, they lost viability rapidly during stationary phase. However, when the bacteria were incubated in these media in the presence of the fungus, their stationary phase survival improved dramatically. On agar plates containing glucose, the beneficial effects of the fungus were manifested in robust bacterial growth and exopolysaccharide production that led to visible mucoidy. In contrast, bacteria grew poorly and were nonmucoid in such media in the absence of the fungus. By using the available S. cerevisiae deletion library, yeast mutants that were unable to mediate this beneficial interaction were identified. These mutants revealed that the beneficial effect on bacterial physiology and survival was mediated by the ability of the fungus to metabolize the available glucose and consequent effects on the medium's pH. In natural environments where the concentration of glucose is high, it is likely that the presence of fungi has had profound beneficial effects on the physiology and survival of certain P. putida strains throughout their natural history.

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 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.

scholarly journals Staphylococcus aureus Aconitase Inactivation Unexpectedly Inhibits Post-Exponential-Phase Growth and Enhances Stationary-Phase Survival

2002 ◽  
Vol 70 (11) ◽  
pp. 6373-6382 ◽  
Author(s):  
Greg A. Somerville ◽  
Michael S. Chaussee ◽  
Carrie I. Morgan ◽  
J. Ross Fitzgerald ◽  
David W. Dorward ◽  
...  
Keyword(s):  
Stationary Phase ◽  
Tca Cycle ◽  
Exponential Growth Phase ◽  
Wild Type ◽  
Phase Growth ◽  
Iron Sulfur Cluster ◽  
Iron Sulfur ◽  
The Tca Cycle ◽  
Stationary Phase Survival ◽  
Virulence Factor Production

ABSTRACT Staphylococcus aureus preferentially catabolizes glucose, generating pyruvate, which is subsequently oxidized to acetate under aerobic growth conditions. Catabolite repression of the tricarboxylic acid (TCA) cycle results in the accumulation of acetate. TCA cycle derepression coincides with exit from the exponential growth phase, the onset of acetate catabolism, and the maximal expression of secreted virulence factors. These data suggest that carbon and energy for post-exponential-phase growth and virulence factor production are derived from the catabolism of acetate mediated by the TCA cycle. To test this hypothesis, the aconitase gene was genetically inactivated in a human isolate of S. aureus, and the effects on physiology, morphology, virulence factor production, virulence for mice, and stationary-phase survival were examined. TCA cycle inactivation prevented the post-exponential growth phase catabolism of acetate, resulting in premature entry into the stationary phase. This phenotype was accompanied by a significant reduction in the production of several virulence factors and alteration in host-pathogen interaction. Unexpectedly, aconitase inactivation enhanced stationary-phase survival relative to the wild-type strain. Aconitase is an iron-sulfur cluster-containing enzyme that is highly susceptible to oxidative inactivation. We speculate that reversible loss of the iron-sulfur cluster in wild-type organisms is a survival strategy used to circumvent oxidative stress induced during host-pathogen interactions. Taken together, these data demonstrate the importance of the TCA cycle in the life cycle of this medically important pathogen.

scholarly journals High-Resolution Profiling of Stationary-Phase Survival Reveals Yeast Longevity Factors and Their Genetic Interactions

PLoS Genetics ◽  
2014 ◽  
Vol 10 (2) ◽  
pp. e1004168 ◽  
Author(s):  
Erika Garay ◽  
Sergio E. Campos ◽  
Jorge González de la Cruz ◽  
Ana P. Gaspar ◽  
Adrian Jinich ◽  
...  
Keyword(s):  
High Resolution ◽  
Stationary Phase ◽  
Genetic Interactions ◽  
Stationary Phase Survival
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