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|Title:||Structural and Biochemical Studies of Proteins Involved in Polyamine Transport from Pseudomonas Aeruginosa PAO1 and mRNA Decay From Saccharomyces Cerevisiae||Authors:||WU DONGHUI||Keywords:||polyamine receptor, substrate specificity, ligand binding induced conformational change, decapping activator, mRNA decay, translational repression||Issue Date:||19-Jan-2010||Citation:||WU DONGHUI (2010-01-19). Structural and Biochemical Studies of Proteins Involved in Polyamine Transport from Pseudomonas Aeruginosa PAO1 and mRNA Decay From Saccharomyces Cerevisiae. ScholarBank@NUS Repository.||Abstract:||This thesis comprises two parts. The first part addresses structural and biochemical studies of proteins involved in polyamine transport in Pseudomonas aeruginosa PAO1. In this study, four structures were solved, spuD in ligand-free open form, spuD in putrescine-bound closed form, spuE in ligand-free open form and spuE in spermidine-bound closed form. This is the first report in which both putresine and spermidine binding proteins in both ligand-free and ligand-bound forms are presented. Comparison of these four structures reveals novel insight into the basis of polyamine binding specificity, as well as direct insight into the conformational changes associated with ligand binding. The second part briefly describes an in vitro assembly of decapping activator Lsm1-7-Pat1-465c eight-protein complex involved in mRNA decay and a preliminary structural study of the carboxyl terminal domain of Pat1 which plays an important role in mRNA decay and translational repression.||URI:||http://scholarbank.nus.edu.sg/handle/10635/18521|
|Appears in Collections:||Ph.D Theses (Open)|
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