Please use this identifier to cite or link to this item: http://scholarbank.nus.edu.sg/handle/10635/17610
Title: X-ray crystallographic study of yeast Dcp1 and Dcp2 proteins: Insights into the mechanism and regulation of eukaryotic mRNA decapping
Authors: SHE MEIPEI
Keywords: mRNA decapping, crystal structure, Dcp1, Dcp2
Issue Date: 8-Oct-2007
Source: SHE MEIPEI (2007-10-08). X-ray crystallographic study of yeast Dcp1 and Dcp2 proteins: Insights into the mechanism and regulation of eukaryotic mRNA decapping. ScholarBank@NUS Repository.
Abstract: mRNA decapping by the Dcp1-Dcp2 complex is a rate-limiting step of the 5a??-3a?? mRNA decay pathway. This thesis presented the crystal structures of individual yeast Dcp1 and Dcp2 proteins and the Dcp1-Dcp2 complex. (1) The S.cerevisiae Dcp1 protein contains an N-terminal extension region and a core EVH1 domain, which is a protein-protein interaction module. (2) The functional region of S. pombe Dcp2 protein consists of an N-terminal helical domain followed by a Nudix domain. The Nudix domain is the catalytic center while N-terminal domain interacts with Dcp1p to stimulate the decapping activity. (3) The crystal structure of S. pombe Dcp1p-Dcp2 N-terminal domain complex reveals that the N-terminal extension of Dcp1p is involved in Dcp2p binding and that the protein-protein interface is yeast specific. The possibility of Dcp1p to bind additional factor was discussed and a model of the assembly and regulation of the 5a??-3a?? mRNA decay machinery was proposed.
URI: http://scholarbank.nus.edu.sg/handle/10635/17610
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