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|Title:||THE MECHANISM OF OSMOSENSING AND TRANSMEMBRANE SIGNAL TRANSDUCTION||Authors:||WANG LOO CHIEN||Keywords:||Amide hydrogen/deuterium exchange, mass spectrometry, dynamics, membrane protein, osmosensing, signal transduction||Issue Date:||22-Aug-2014||Citation:||WANG LOO CHIEN (2014-08-22). THE MECHANISM OF OSMOSENSING AND TRANSMEMBRANE SIGNAL TRANSDUCTION. ScholarBank@NUS Repository.||Abstract:||Signal sensing is the key step in cells coordinating responses to stresses, but the molecular details of sensing are less understood. Using bacterial osmoregulation as a model, the conformational dynamics of the inner membrane protein and sensor histidine kinase EnvZ in response to osmolytes was investigated. The results reveal that EnvZ is conformationally dynamic under low osmolality conditions. At high osmolality, it is shifted to favor a more folded state, facilitating enhanced activities. They also reveal that the cytoplasmic domain of EnvZ alone is capable and sufficient for osmosensing. The functions of EnvZ are modulated by key communications between main chain dynamics and side chain interactions. Membrane anchoring is also shown to increase the dynamics of EnvZ, suggesting that an autoinhibitory regulatory role. Taken together, a local unfolding model for EnvZ osmosensing is proposed. These studies also show that the conformational dynamics of a receptor protein is imperative for signal sensing and transduction.||URI:||http://scholarbank.nus.edu.sg/handle/10635/119598|
|Appears in Collections:||Ph.D Theses (Open)|
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