crystal structure of the rna recognition motif of yeast translation initiation factor eif3b reveals differences to human eif3b晶体结构酵母rna识别主题的翻译起始因子对人类eif3b eif3b显示差异.pdfVIP

crystal structure of the rna recognition motif of yeast translation initiation factor eif3b reveals differences to human eif3b晶体结构酵母rna识别主题的翻译起始因子对人类eif3b eif3b显示差异.pdf

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crystal structure of the rna recognition motif of yeast translation initiation factor eif3b reveals differences to human eif3b晶体结构酵母rna识别主题的翻译起始因子对人类eif3b eif3b显示差异

Crystal Structure of the RNA Recognition Motif of Yeast Translation Initiation Factor eIF3b Reveals Differences to Human eIF3b Sohail Khoshnevis, Piotr Neumann, Ralf Ficner* ¨ ¨ Department of Molecular Structural Biology, Institute of Microbiology and Genetics, Georg-August University Gottingen, Gottingen, Germany Abstract Background: The multi-subunit eukaryotic initiation factor3 (eIF3) plays a central role in the initiation step of protein synthesis in eukaryotes. One of its large subunits, eIF3b, serves as a scaffold within eIF3 as it interacts with several other subunits. It harbors an RNA Recognition Motif (RRM), which is shown to be a non-canonical RRM in human as it is not capable to interact with oligonucleotides, but rather interacts with eIF3j, a sub-stoichiometric subunit of eIF3. Principal Finding: We have analyzed the high-resolution crystal structure of the eIF3b RRM domain from yeast. It exhibits the same fold as its human ortholog, with similar charge distribution on the surface interacting with the eIF3j in human. Thermodynamic analysis of the interaction between yeast eIF3b-RRM and eIF3j revealed the same range of enthalpy change and dissociation constant as for the human proteins, providing another line of evidence for the same mode of interaction between eIF3b and eIF3j in both organisms. However, analysis of the surface charge distribution of the putative RNA-binding b-sheet suggested that in contrast to its human ortholog, it potentially could bind oligonucleotides. Three-dimensional positioni

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