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Title: Structural and functional analysis of critical proteins involved in mRNA decay
Keywords: mRNA decay, nonsense-mediated mRNA decay, WD-repeat protein, Ski8, DEAD-box protein, Dhh1, RNA helicase, Upf1, X-ray crystallography
Issue Date: 26-Feb-2007
Citation: CHENG ZHIHONG (2007-02-26). Structural and functional analysis of critical proteins involved in mRNA decay. ScholarBank@NUS Repository.
Abstract: mRNA degradation is important for gene expression in eukaryotic cells. Three proteins, Ski8, Dhh1 and hUpf1 involved in mRNA decay, have been structurally and functionally studied. Ski8, a WD-repeat protein, plays an essential role in 3'-to-5' mRNA decay. Crystal structure of Ski8 shows a seven-bladed i??-propeller with the top face revealed to be involved in protein-protein interaction by structural and mutagenesis analysis. Dhh1, a DEAD-box protein, functions both to repress translation and enhance decapping. The structure of the truncated Dhh1 represents a two RecA-like architecture with a unique arrangement. A conformational change and a prominent RNA binding site have been identified by structural analysis combined with mutagenesis studies. Upf1, a SF1 RNA helicase, plays a critical role in nonsense-mediated mRNA decay. Crystal structures of the catalytic core of human Upf1 determined in three states (phosphate-, AMPPNP- and ADP-bound forms) reveal an overall structure composed of two RecA-like domains with two additional domains protruding from the N-terminal RecA-like domain. Structural analysis combined with mutagenesis studies presented a likely ssRNA binding channel, a cycle of conformational change coupled to ATP binding/hydrolysis and a mechanism of ATP-modulated RNA binding.
Appears in Collections:Ph.D Theses (Open)

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