crystal structures of lsm3, lsm4 and lsm567 from schizosaccharomyces pombe晶体结构的lsm3,lsm4 lsm567粟酒裂殖酵母.pdf

Crystal Structures of Lsm3, Lsm4 and Lsm5/6/7 from Schizosaccharomyces pombe 1. 1. 3 1,2,4 Donghui Wu , Shimin Jiang , Matthew W. Bowler , Haiwei Song * 1 Institute of Molecular and Cell Biology, Singapore, Singapore, 2 Life Sciences Institute and School of Medicine, Zhejiang University, Hangzhou, China, 3 Structural Biology Group, European Synchrotron Radiation Facility, Grenoble, France, 4 Department of Biochemistry, National University of Singapore, Singapore, Singapore Abstract Sm-like (Lsm) proteins are ubiquitous and function in many aspects of RNA metabolism, including pre-mRNA splicing, nuclear RNA processing, mRNA decay and miRNA biogenesis. Here three crystal structures including Lsm3, Lsm4 and Lsm5/ 6/7 sub-complex from S. pombe are reported. These structures show that all the five individual Lsm subunits share a conserved Sm fold, and Lsm3, Lsm4, and Lsm5/6/7 form a heptamer, a trimer and a hexamer within the crystal lattice, respectively. Analytical ultracentrifugation indicates that Lsm3 and Lsm5/6/7 sub-complex exist in solution as a heptamer and a hexamer, respectively while Lsm4 undergoes a dynamic equilibrium between monomer and trimer in solution. RNA binding assays show that Lsm2/3 and Lsm5/6/7 bind to oligo(U) whereas no RNA binding is observed for Lsm3 and Lsm4. Analysis of the inter-subunit interactions in Lsm5/6/7 reveals the organization order among Lsm5, Lsm6 and Lsm7. Citation: Wu D, Jiang S, Bowler MW, Song H (2012) Crystal Structures of Lsm3, Lsm4 and Lsm5/6/7 from Schizosaccharomyces pombe. PLoS ONE 7(5): e36768. doi:10.1371/journal.pone.0036768 Editor: P