Three-dimensional cryo-electron microscopy localization of EF2 in the Saccharomyces cerevisiae 80S ribosome at 17.5 Å resolution

被引：134
作者：
Gomez-Lorenzo, MG
Spahn, CMT
Agrawal, RK
Grassucci, RA
Penczek, P
Chakraburtty, K
Ballesta, JPG
Lavandera, JL
Garcia-Bustos, JF
Frank, J
机构：
[1] SUNY Albany, Wadsworth Ctr, Howard Hughes Med Inst, Hlth Res Inc, Albany, NY 12201 USA
[2] SUNY Albany, Dept Biomed Sci, Albany, NY 12201 USA
[3] Med Coll Wisconsin, Dept Biochem, Milwaukee, WI 53226 USA
[4] Glaxo Wellcome SA, Res Dept, Tres Cantos, Spain
[5] CSIC, Ctr Biol Mol Severo Ochoa, E-28049 Madrid, Spain
[6] Univ Autonoma Madrid, E-28049 Madrid, Spain
来源：
EMBO JOURNAL | 2000年 / 19卷 / 11期
关键词：
elongation; GM193663; sordarin; translation; yeast;
D O I：
10.1093/emboj/19.11.2710
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：
Using a sordarin derivative, an antifungal drug, it was possible to determine the structure of a eukaryotic ribosome-EF2 complex at 17.5 Angstrom resolution by three-dimensional (3D) cryo-electron microscopy. EF2 is directly visible in the 3D map and the overall arrangement of the complex from Saccharomyces cerevisiae corresponds to that previously seen in Escherichia coli, However, pronounced differences were found in two prominent regions. First, in the yeast system the interaction between the elongation factor and the stalk region of the large subunit is much more extensive. Secondly, domain IV of EF2 contains additional mass that appears to interact with the head of the 40S subunit and the region of the main bridge of the 60S subunit, The shape and position of domain IV of EF2 suggest that it might interact directly with P-site-bound tRNA.
引用
收藏
页码：2710 / 2718
页数：9
相关论文
共 59 条
[31]   Escherichia coli 70 S ribosome at 15 Å resolution by cryo-electron microscopy:: Localization of fMet-tRNAfMet and fitting of L1 protein [J].
Malhotra, A ;
Penczek, P ;
Agrawal, RK ;
Gabashvili, IS ;
Grassucci, RA ;
Jünemann, R ;
Burkhardt, N ;
Nierhaus, KH ;
Frank, J .
JOURNAL OF MOLECULAR BIOLOGY, 1998, 280 (01) :103-116
[32]   Domain IV of elongation factor G from Thermus thermophilus is strictly required for translocation [J].
Martemyanov, KA ;
Gudkov, AT .
FEBS LETTERS, 1999, 452 (03) :155-159
[33]   INTERACTION OF ELONGATION-FACTORS EF-G AND EF-TU WITH A CONSERVED LOOP IN 23S RNA [J].
MOAZED, D ;
ROBERTSON, JM ;
NOLLER, HF .
NATURE, 1988, 334 (6180) :362-364
[34]  
Moller W., 1986, STRUCTURE FUNCTION G, P309
[35]   THE CONSERVED GTPASE CENTER AND VARIABLE REGION V9 FROM SACCHAROMYCES-CEREVISIAE 26S RIBOSOMAL-RNA CAN BE REPLACED BY THEIR EQUIVALENTS FROM OTHER PROKARYOTES OR EUKARYOTES WITHOUT DETECTABLE LOSS OF RIBOSOMAL FUNCTION [J].
MUSTERS, W ;
GONCALVES, PM ;
BOON, K ;
RAUE, HA ;
VANHEERIKHUIZEN, H ;
PLANTA, RJ .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1991, 88 (04) :1469-1473
[36]   CRYSTAL-STRUCTURE OF THE TERNARY COMPLEX OF PHE-TRNA(PHE), EF-TU, AND A GTP ANALOG [J].
NISSEN, P ;
KJELDGAARD, M ;
THIRUP, S ;
POLEKHINA, G ;
RESHETNIKOVA, L ;
CLARK, BFC ;
NYBORG, J .
SCIENCE, 1995, 270 (5241) :1464-1472
[37]  
OPPENHEIMER NJ, 1981, J BIOL CHEM, V256, P8579
[38]   Structure of keyhole limpet hemocyanin type 1 (KLH1) at 15 angstrom resolution by electron cryomicroscopy and angular reconstitution [J].
Orlova, EV ;
Dube, P ;
Harris, JR ;
Beckman, E ;
Zemlin, F ;
Markl, J ;
vanHeel, M .
JOURNAL OF MOLECULAR BIOLOGY, 1997, 271 (03) :417-437
[39]   THE RIBOSOME AT IMPROVED RESOLUTION - NEW TECHNIQUES FOR MERGING AND ORIENTATION REFINEMENT IN 3D CRYOELECTRON MICROSCOPY OF BIOLOGICAL PARTICLES [J].
PENCZEK, PA ;
GRASSUCCI, RA ;
FRANK, J .
ULTRAMICROSCOPY, 1994, 53 (03) :251-270
[40]  
REMACHA M, 1995, MOL CELL BIOL, V15, P4754
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