Coordinate control of virulence gene expression in francisella tularensis
TL;DRAbstract
Francisella tularensis is a Gram-negative, intracellular pathogen and the causative agent of tularemia. Due to its low infectious dose, ability to cause potentially fatal disease, and ability to be easily aerosolized, several countries have developed F. tularensis as a potential bioweapon. Three proteins, MglA, SspA, and PigR, and the small molecule guanosine tetraphosphate (ppGpp), are transcription factors critical for the virulence of this organism. These regulators function coordinately to positively regulate the expression of genes present on the Francisella pathogenicity island, as well as many other genes that are required for the virulence of this organism. MglA and SspA form a complex that associates with RNA polymerase (RNAP); the interaction between the MglA-SspA complex and RNAP is thought to be critical for MglA and SspA to regulate gene expression. PigR, a putative DNA-binding protein, associates with the RNAP-associated MglA-SspA complex and may stabilize the binding of
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Francisella tularensis is a Gram-negative, intracellular pathogen and the causative agent of tularemia. Due to its low infectious dose, ability to cause potentially fatal disease, and ability to be easily aerosolized, several countries have developed F. tularensis as a potential bioweapon. Three proteins, MglA, SspA, and PigR, and the small molecule guanosine tetraphosphate (ppGpp), are transcription factors critical for the virulence of this organism. These regulators function coordinately to positively regulate the expression of genes present on the Francisella pathogenicity island, as well as many other genes that are required for the virulence of this organism. MglA and SspA form a complex that associates with RNA polymerase (RNAP); the interaction between the MglA-SspA complex and RNAP is thought to be critical for MglA and SspA to regulate gene expression. PigR, a putative DNA-binding protein, associates with the RNAP-associated MglA-SspA complex and may stabilize the binding of
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