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Studies of the Full-length Histidine Kinase VanSA in Detergent: From Sensing Vancomycin to Regulating its Response Regulator, VanRA
Başlık:
Studies of the Full-length Histidine Kinase VanSA in Detergent: From Sensing Vancomycin to Regulating its Response Regulator, VanRA
Yazar:
Upton, Elizabeth C., author.
ISBN:
9780438148321
Yazar Ek Girişi:
Fiziksel Tanımlama:
1 electronic resource (167 pages)
Genel Not:
Source: Dissertation Abstracts International, Volume: 79-11(E), Section: B.
Advisors: Patrick J. Loll Committee members: Simon Cocklin; Mark Goulian; Eileen Jaffe; Marilyn Jorns.
Özet:
VanSA is a sensor histidine kinase responsible for detecting vancomycin and activating expression of vancomycin-resistance genes in vancomycin-resistant bacteria. When VanSA senses vancomycin it autophosphorylates and then transfers that phosphate to the transcription factor VanRA. Phospho-VanRA then activates transcription of the enzymes that remodel the cell wall to avert vancomycin's effects. In the absence of vancomycin VanSA has a third enzymatic activity, phosphatase activity, which it uses to maintain VanRA in an inactivated state. This is required because VanRA can be non-specifically phosphorylated by small molecule phospho-donors and, potentially, other histidine kinases (referred to as cross-talk). To study this VanRSA signaling system we purified the individual components including the full-length VanS A protein solubilized in detergent. An ongoing question in the field is whether VanSA detects vancomycin directly or detects a downstream effect of vancomycin. We found that vancomycin does not affect the activity of purified full-length VanSA in detergent. We also found that a non-partner histidine kinase, PhoR, phosphorylates VanR A much more slowly than its cognate partner VanSA does. PhoR binds VanRA with an affinity comparable to that of VanSA, indicating that the binding affinity alone does not confer partner-like signaling.
Notlar:
School code: 0065
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