Structural basis of highly conserved ribosome recycling in eukaryotes and archaea

被引:191
作者
Becker, Thomas [1 ,2 ]
Franckenberg, Sibylle [1 ,2 ]
Wickles, Stephan [1 ,2 ]
Shoemaker, Christopher J. [3 ]
Anger, Andreas M. [1 ,2 ]
Armache, Jean-Paul [1 ,2 ]
Sieber, Heidemarie [1 ,2 ]
Ungewickell, Charlotte [1 ,2 ]
Berninghausen, Otto [1 ,2 ]
Daberkow, Ingo
Karcher, Annette [1 ,2 ,4 ]
Thomm, Michael [5 ,6 ]
Hopfner, Karl-Peter [1 ,2 ]
Green, Rachel [3 ]
Beckmann, Roland [1 ,2 ]
机构
[1] Univ Munich, Dept Biochem, Gene Ctr, D-81377 Munich, Germany
[2] Univ Munich, Dept Biochem, Ctr Integrated Prot Sci Munich CiPSM, D-81377 Munich, Germany
[3] Johns Hopkins Univ, Sch Med, Dept Mol Biol & Genet, Howard Hughes Med Inst, Baltimore, MD 21205 USA
[4] Tietz Video & Image Proc Syst GmbH, D-82131 Gauting, Germany
[5] Univ Icking, D-82057 Icking, Germany
[6] Univ Regensburg, Dept Microbiol, NWF Biol & Preclin Med 3, D-93053 Regensburg, Germany
基金
美国国家卫生研究院;
关键词
MESSENGER-RNA DECAY; NO-GO DECAY; FREE PROTEIN-SYNTHESIS; X-RAY-STRUCTURE; ATP-BINDING; TRANSLATION TERMINATION; ELECTRON-MICROSCOPY; CRYSTAL-STRUCTURE; 80S RIBOSOME; THERMOCOCCUS-KODAKARAENSIS;
D O I
10.1038/nature10829
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Ribosome-driven protein biosynthesis is comprised of four phases: initiation, elongation, termination and recycling. In bacteria, ribosome recycling requires ribosome recycling factor and elongation factor G, and several structures of bacterial recycling complexes have been determined. In the eukaryotic and archaeal kingdoms, however, recycling involves the ABC-type ATPase ABCE1 and little is known about its structural basis. Here we present cryo-electron microscopy reconstructions of eukaryotic and archaeal ribosome recycling complexes containing ABCE1 and the termination factor paralogue Pelota. These structures reveal the overall binding mode of ABCE1 to be similar to canonical translation factors. Moreover, the iron-sulphur cluster domain of ABCE1 interacts with and stabilizes Pelota in a conformation that reaches towards the peptidyl transferase centre, thus explaining how ABCE1 may stimulate peptide-release activity of canonical termination factors. Using the mechanochemical properties of ABCE1, a conserved mechanism in archaea and eukaryotes is suggested that couples translation termination to recycling, and eventually to re-initiation.
引用
收藏
页码:501 / U221
页数:8
相关论文
共 56 条
[21]  
Eswar Narayanan, 2008, V426, P145, DOI 10.1007/978-1-60327-058-8_8
[22]   SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields [J].
Frank, J ;
Radermacher, M ;
Penczek, P ;
Zhu, J ;
Li, YH ;
Ladjadj, M ;
Leith, A .
JOURNAL OF STRUCTURAL BIOLOGY, 1996, 116 (01) :190-199
[23]   An mRNA surveillance mechanism that eliminates transcripts lacking termination codons [J].
Frischmeyer, PA ;
van Hoof, A ;
O'Donnell, K ;
Guerrerio, AL ;
Parker, R ;
Dietz, HC .
SCIENCE, 2002, 295 (5563) :2258-2261
[24]   Mutations in the highly conserved GGQ motif of class 1 polypeptide release factors abolish ability of human eRF1 to trigger peptidyl-tRNA hydrolysis [J].
Frolova, LY ;
Tsivkovskii, RY ;
Sivolobova, GF ;
Oparina, NY ;
Serpinsky, OI ;
Blinov, VM ;
Tatkov, SI ;
Kisselev, LL .
RNA, 1999, 5 (08) :1014-1020
[25]   The Structure of the Ribosome with Elongation Factor G Trapped in the Posttranslocational State [J].
Gao, Yong-Gui ;
Selmer, Maria ;
Dunham, Christine M. ;
Weixlbaumer, Albert ;
Kelley, Ann C. ;
Ramakrishnan, V. .
SCIENCE, 2009, 326 (5953) :694-699
[26]   Structure of yeast Dom34 - A protein related to translation termination factor eRF1 and involved in No-Go decay [J].
Graille, Marc ;
Chaillet, Maxime ;
van Tilbeurgh, Herman .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2008, 283 (11) :7145-7154
[27]   Rad50/SMC proteins and ABC transporters: unifying concepts from high-resolution structures [J].
Hopfner, KP ;
Tainer, JA .
CURRENT OPINION IN STRUCTURAL BIOLOGY, 2003, 13 (02) :249-255
[28]   Translation termination factor eRF3 mediates mRNA decay through the regulation of deadenylation [J].
Hosoda, N ;
Kobayashi, T ;
Uchida, N ;
Funakoshi, Y ;
Kikuchi, Y ;
Hoshino, S ;
Katada, T .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (40) :38287-38291
[29]   X-Ray structure of RLI, an essential twin cassette ABC ATPase involved in ribosome biogenesis and HIV capsid assembly [J].
Karcher, A ;
Büttner, K ;
Märtens, B ;
Jansen, RP ;
Hopfner, KP .
STRUCTURE, 2005, 13 (04) :649-659
[30]   X-ray structure of the complete ABC enzyme ABCE1 from Pyrococcus abyssi [J].
Karcher, Annette ;
Schele, Alexandra ;
Hopfner, Karl-Peter .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2008, 283 (12) :7962-7971