small ribosomal protein rps0 stimulates translation initiation by mediating 40s-binding of eif3 via its direct contact with the eif3atif32 subunit小核糖体蛋白rps0刺激翻译起始的调停40 s-binding eif3 eif3atif32亚基通过直接接触.pdf

Small Ribosomal Protein RPS0 Stimulates Translation Initiation by Mediating 40S-Binding of eIF3 via Its Direct Contact with the eIF3a/TIF32 Subunit ´ ˇ 1. ´ ´ 1. ˇ ´ 1 ´ 1 ˇ ´ 1 Tomas Kouba , Istvan Danyi , Stanislava Gunisova , Vanda Munzarova , Vladislava Vlc kova , ´ 1 2 2 ˇ ´ ˇ 1 Lucie Cuchalova , Andreas Neueder , Philipp Milkereit , Leos Shivaya Valasek * ¨ 1 Laboratory of Regulation of Gene Expression, Institute of Microbiology ASCR, v.v.i., Prague, The Czech Republic, 2 Institut fur Biochemie, Genetik und Mikrobiologie, University of Regensburg, Regensburg, Germany Abstract The ribosome translates information encoded by mRNAs into proteins in all living cells. In eukaryotes, its small subunit together with a number of eukaryotic initiation factors (eIFs) is responsible for locating the mRNA’s translational start to properly decode the genetic message that it carries. This multistep process requires timely and spatially coordinated placement of eIFs on the ribosomal surface. In our long-standing pursuit to map the 40S-binding site of one of the functionally most complex eIFs, yeast multisubunit eIF3, we identified several interactions that placed its major body to the head, beak and shoulder regions of the solvent-exposed side of the 40S subunit. Among them is the interaction bet