Role of the C-terminal cytoplasmic tail of the NhaP2 antiporter from Vibrio cholerae in transmembrane ion transport
| dc.contributor.author | Wiens, Evan Jonathan | |
| dc.contributor.examiningcommittee | Dibrov, Pavel (Microbiology) McKenna, Sean (Chemistry) Khajehpour, Mazdak (Chemistry) | en_US |
| dc.contributor.supervisor | Stetefeld, Joerg (Chemistry) | en_US |
| dc.date.accessioned | 2013-09-16T15:35:15Z | |
| dc.date.available | 2013-09-16T15:35:15Z | |
| dc.date.issued | 2013-09-16 | |
| dc.degree.discipline | Chemistry | en_US |
| dc.degree.level | Master of Science (M.Sc.) | en_US |
| dc.description.abstract | Although the importance of cation/proton antiporters in cellular physiology is well recognized and widely studied, many antiport systems remain underinvestigated. In this work, I report the phenotypic and biochemical effects of deletion of the cytoplasmic C-terminal tail of the NhaP2 antiporter from Vibrio cholerae (Vc-NhaP2). Namely, deletion of the C-terminal tail results in diminished K+/H+ and Na+/H+ antiport activity, as well as a 5-fold decrease in affinity for its major substrate, K+ (measured as the apparent Km at pH 7.5). Furthermore, reconstitution of antiport activity in the truncation mutant upon addition of exogenous C-terminal tail is demonstrated. Currently, the only known mechanism of antiport is for NhaA, which lacks a cytoplasmic tail. Therefore, these results suggest that NhaP2 may employ a novel mechanism of antiport in which the cytoplasmic tail is directly or indirectly involved. | en_US |
| dc.description.note | October 2013 | en_US |
| dc.identifier.uri | http://hdl.handle.net/1993/22193 | |
| dc.language.iso | eng | en_US |
| dc.rights | open access | en_US |
| dc.subject | Sodium-proton antiport | en_US |
| dc.subject | Potassium-proton antiport | en_US |
| dc.subject | Vibrio cholerae | en_US |
| dc.title | Role of the C-terminal cytoplasmic tail of the NhaP2 antiporter from Vibrio cholerae in transmembrane ion transport | en_US |
| dc.type | master thesis | en_US |