Isolation and Preliminary Characterization of Amino Acid Substitution Mutations That Increase the Activity of the Osmoregulated ProP Protein of Salmonella Enterica Serovar Typhimurium

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 select...

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Detalhes bibliográficos
Main Authors: 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.
Formato: Artigo
Idioma:Inglês
Publicado em: Mary Ann Liebert, Inc. 2012
Assuntos:
Original Research Articles by Undergraduates
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC3378968/
https://ncbi.nlm.nih.gov/pubmed/22360681
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1089/dna.2011.1510
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