Structure of the mammalian 80S ribosome at 8.7 Å resolution

被引:117
作者
Chandramouli, Preethi [2 ]
Topf, Maya [1 ]
Menetret, Jean-Francois [2 ]
Eswar, Narayanan [3 ]
Cannone, Jamie J. [4 ]
Gutell, Robin R. [4 ]
Sali, Andrej [3 ]
Akey, Christopher W. [2 ]
机构
[1] Univ London Birkbeck Coll, Sch Crystallog, London WC1E 7HX, England
[2] Boston Univ, Sch Med, Dept Phys & Biophys, Boston, MA 02118 USA
[3] Univ Calif San Francisco, California Inst Quantitat Biomed Res, Dept Biopharmaceut Sci, San Francisco, CA 94158 USA
[4] Univ Texas Austin, Inst Cellular & Mol Biol, Austin, TX 78712 USA
基金
英国医学研究理事会;
关键词
D O I
10.1016/j.str.2008.01.007
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
In this paper, we present a structure of the mammalian ribosome determined at similar to 8.7 angstrom resolution by electron cryomicroscopy and single-particle methods. A model of the ribosome was created by docking homology models of subunit rRNAs and conserved proteins into the density map. We then modeled expansion segments in the subunit rRNAs and found unclaimed density for similar to 20 proteins. In general, many conserved proteins and novel proteins interact with expansion segments to form an integrated framework that may stabilize the mature ribosome. Our structure provides a snapshot of the mammalian ribosome at the beginning of translation and lends support to current models in which large movements of the small subunit and L1 stalk occur during tRNA translocation. Finally, details are presented for intersubunit bridges that are specific to the eukaryotic ribosome. We suggest that these bridges may help reset the conformation of the ribosome to prepare for the next cycle of chain elongation.
引用
收藏
页码:535 / 548
页数:14
相关论文
共 59 条
[1]   The cryo-EM structure of a translation initiation complex from Escherichia coli [J].
Allen, GS ;
Zavialov, A ;
Gursky, R ;
Ehrenberg, M ;
Frank, J .
CELL, 2005, 121 (05) :703-712
[2]   Structure of eEF3 and the mechanism of transfer RNA release from the E-site [J].
Andersen, Christian B. F. ;
Becker, Thomas ;
Blau, Michael ;
Anand, Monika ;
Halic, Mario ;
Balar, Bharvi ;
Mielke, Thorsten ;
Boesen, Thomas ;
Pedersen, Jan Skov ;
Spahn, Christian M. T. ;
Kinzy, Terri Goss ;
Andersen, Gregers R. ;
Beckmann, Roland .
NATURE, 2006, 443 (7112) :663-668
[3]   Architecture of the protein-conducting channel associated with the translating 80S ribosome [J].
Beckmann, R ;
Spahn, CMT ;
Eswar, N ;
Helmers, J ;
Penczek, PA ;
Sali, A ;
Frank, J ;
Blobel, G .
CELL, 2001, 107 (03) :361-372
[4]   Insights into protein biosynthesis from structures of bacterial ribosomes [J].
Berk, Veysel ;
Cate, Jamie H. D. .
CURRENT OPINION IN STRUCTURAL BIOLOGY, 2007, 17 (03) :302-309
[5]   Structural basis for mRNA and tRNA positioning on the ribosome [J].
Berk, Veysel ;
Zhang, Wen ;
Pai, Raj D. ;
Cate, Jamie H. Doudna .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2006, 103 (43) :15830-15834
[6]   The structural basis for the action of the antibiotics tetracycline, pactamycin, and hygromycin B on the 30S ribosomal subunit [J].
Brodersen, DE ;
Clemons, WM ;
Carter, AP ;
Morgan-Warren, RJ ;
Wimberly, BT ;
Ramakrishnan, V .
CELL, 2000, 103 (07) :1143-1154
[7]   Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics [J].
Carter, AP ;
Clemons, WM ;
Brodersen, DE ;
Morgan-Warren, RJ ;
Wimberly, BT ;
Ramakrishnan, V .
NATURE, 2000, 407 (6802) :340-348
[8]   Release of eIF6 (p27BBP) from the 60S subunit allows 80S ribosome assembly [J].
Ceci, M ;
Gaviraghi, C ;
Gorrini, C ;
Sala, LA ;
Offenhäuser, N ;
Marchisio, PC ;
Biffo, S .
NATURE, 2003, 426 (6966) :579-584
[9]   Proteomic characterization of evolutionarily conserved and variable proteins of arabidopsis cytosolic ribosomes [J].
Chang, IF ;
Szick-Miranda, K ;
Pan, SQ ;
Bailey-Serres, J .
PLANT PHYSIOLOGY, 2005, 137 (03) :848-862
[10]   Interaction of the G′ domain of elongation factor G and the C-terminal domain of ribosomal protein L7/L12 during translocation as revealed by cryo-EM [J].
Datta, PP ;
Sharma, MR ;
Qi, L ;
Frank, J ;
Agrawal, RK .
MOLECULAR CELL, 2005, 20 (05) :723-731