transport mutant
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Author(s):  
Erin M. Vasicek ◽  
Lindsey O’Neal ◽  
Matthew R. Parsek ◽  
James Fitch ◽  
Peter White ◽  
...  

L-arabinose inducible promoters are commonly used in gene expression analysis. However, nutrient source and availability also play a role in biofilm formation; therefore, L-arabinose metabolism could impact biofilm development. In this study we examined the impact of L-arabinose on Salmonella enterica serovar Typhimurium (S. Typhimurium) biofilm formation. Using mutants impaired for the transport and metabolism of L-arabinose, we showed that L-arabinose metabolism negatively impacts S. Typhimurium biofilm formation in vitro. When L-arabinose metabolism is abrogated, biofilm formation returned to baseline levels. However, without the ability to import extracellular L-arabinose, biofilm formation significantly increased. Using RNA-Seq we identified several gene families involved in these different phenotypes including curli expression, amino acid synthesis, and L-arabinose metabolism. Several individual candidate genes were tested for their involvement in the L-arabinose-mediated biofilm phenotypes, but most played no significant role. Interestingly, in the presence of L-arabinose the diguanylate cyclase gene adrA was downregulated in wild type S. Typhimurium. Meanwhile cyaA, encoding an adenylate cyclase, was downregulated in an L-arabinose transport mutant. Using an IPTG-inducible plasmid to deplete c-di-GMP via vieA expression, we were able to abolish the increased biofilm phenotype seen in the transport mutant. However, the mechanism by which the L-arabinose import mutant forms significantly larger biofilms remains to be determined. Regardless, these data suggest that L-arabinose metabolism influences intracellular c-di-GMP levels and therefore biofilm formation. These findings are important when considering the use of an L-arabinose inducible promoter in biofilm conditions.





2015 ◽  
Vol 26 (2) ◽  
pp. 350-358 ◽  
Author(s):  
Nicole L. Umberger ◽  
Tamara Caspary ◽  
Monica Bettencourt-Dias

Primary cilia are built and maintained by intraflagellar transport (IFT), whereby the two IFT complexes, IFTA and IFTB, carry cargo via kinesin and dynein motors for anterograde and retrograde transport, respectively. Many signaling pathways, including platelet- derived growth factor (PDGF)-AA/αα, are linked to primary cilia. Active PDGF-AA/αα signaling results in phosphorylation of Akt at two residues: P-AktT308 and P-AktS473, and previous work showed decreased P-AktS473 in response to PDGF-AA upon anterograde transport disruption. In this study, we investigated PDGF-AA/αα signaling via P-AktT308 and P-AktS473 in distinct ciliary transport mutants. We found increased Akt phosphorylation in the absence of PDGF-AA stimulation, which we show is due to impaired dephosphorylation resulting from diminished PP2A activity toward P-AktT308. Anterograde transport mutants display low platelet-derived growth factor receptor (PDGFR)α levels, whereas retrograde mutants exhibit normal PDGFRα levels. Despite this, neither shows an increase in P-AktS473 or P-AktT308 upon PDGF-AA stimulation. Because mammalian target of rapamycin complex 1 (mTORC1) signaling is increased in ciliary transport mutant cells and mTOR signaling inhibits PDGFRα levels, we demonstrate that inhibition of mTORC1 rescues PDGFRα levels as well as PDGF-AA–dependent phosphorylation of AktS473 and AktT308 in ciliary transport mutant MEFs. Taken together, our data indicate that the regulation of mTORC1 signaling and PP2A activity by ciliary transport plays key roles in PDGF-AA/αα signaling.



2012 ◽  
Vol 1 (2) ◽  
pp. 182-193 ◽  
Author(s):  
Samuel Gelis ◽  
Miguel Curto ◽  
Luis Valledor ◽  
Asier González ◽  
Joaquín Ariño ◽  
...  




Gene ◽  
2000 ◽  
Vol 254 (1-2) ◽  
pp. 87-96 ◽  
Author(s):  
Jaekwon Lee ◽  
Joseph R. Prohaska ◽  
Susan L. Dagenais ◽  
Thomas W. Glover ◽  
Dennis J. Thiele


1999 ◽  
Vol 22 (9) ◽  
pp. 1169-1175 ◽  
Author(s):  
Miguel A. Quiñones ◽  
Aurora Galván ◽  
Emilio Fernández ◽  
Pedro J. Aparicio


1998 ◽  
Vol 92 (5-6) ◽  
pp. 475-476
Author(s):  
S. O'Regan ◽  
N. Cha ◽  
V. Matz ◽  
F.-M. Meunier




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