Article
Isolation and preliminary characterization of amino acid substitution mutations that increase the activity of the osmoregulated ProP protein of Salmonella enterica serovar Typhimurium.
DNA and cell biology - 1 Jun 2012
Gasper Brittany J, McCreight Jennifer C, Banschbach Katelyn, Bustion Annamarie, Davis Chelsea, Divecha Rohan, Donoho Madison, Elmore Amanda G, Garrison Curtis M, Glenn Steve, Goeman Danielle C, Haby Michelle, Hooks Terrice, Korman Abraham M, Kowal Joseph, Kuschke Samantha, Mellencamp Jane E, Meyer Melanie, Myers Alake N, Nichols Monique F, Pfeifer Allison, Porucznik Alexander, Qu Xiao, Ramos-Miller Margaret, Reed Russell R, Sagintayev Adlet, Singel Joshua M, Smith Anna, Valle Madeline E, Venderley Anne, Weber Chelsea A, Zaffino Anthony J, Csonka Laszlo N, Gardner Stephanie M
Abstract excerpt
In Enterobacteriaceae, the ProP protein, which takes up proline and glycine betaine, is subject to a post-translational control mechanism that increases its activity at high osmolarity. In order to investigate the osmoregulatory mechanism of the Salmonella enterica ProP, we devised a positive selection for mutations that conferred increased activity on this protein at low osmolarity. The selection involved the...
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