Ribosomal crystallography: a flexible nucleotide anchoring tRNA translocation facilitates peptide-bond formation, chirality discrimination and antibiotics synergism

被引：36

作者：

Agmon, I

Amit, M

Auerbach, T

Bashan, A

Baram, D

Bartels, H

Berisio, R

Greenberg, I

Harms, J

Hansen, HAS

Kessler, M

Pyetan, E

Schluenzen, F

Sittner, A

Yonath, A ^{[1
]}

Zarivach, R

机构：

[1] Weizmann Inst Sci, Dept Biol Struct, IL-76100 Rehovot, Israel

[2] Max Planck Res Unit Ribosomal Struct, D-22603 Hamburg, Germany

来源：

FEBS LETTERS | 2004年 / 567卷 / 01期

关键词：

ribosome; peptide-bond formation; positional catalysis; antibiotics synergism; synercid; azithromycin; dual binding;

D O I：

10.1016/j.febslet.2004.03.065

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：

The linkage between internal ribosomal symmetry and transfer RNA (tRNA) positioning confirmed positional catalysis of amino-acid polymerization. Peptide bonds are formed concurrently with tRNA-3' end rotatory motion, in conjunction with the overall messenger RNA (mRNA)/tRNA translocation. Accurate substrate alignment, mandatory for the processivity of protein biosynthesis, is governed by remote interactions. Inherent flexibility of a conserved nucleotide, anchoring the rotatory motion, facilitates chirality discrimination and antibiotics synergism. Potential tRNA interactions explain the universality of the tRNA CCA-end and P-site preference of initial tRNA. The interactions of protein L2 tail with the symmetry-related region periphery explain its conservation and its contributions to nascent chain elongation. (C) Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.

引用

页码：20 / 26

页数：7

共 53 条

[1] On peptide bond formation, translocation, nascent protein progression and the regulatory properties of ribosomes - Delivered on 20 October 2002 at the 28th FEBS Meeting in Istanbul
Agmon, I
Auerbach, T
Baram, D
Bartels, H
Bashan, A
Berisio, R
Fucini, P
Hansen, HAS
Harms, J
Kessler, M
Peretz, M
Schluenzen, F
Yonath, A
Zarivach, R
[J]. EUROPEAN JOURNAL OF BIOCHEMISTRY, 2003, 270 (12): : 2543 - 2556
[2] AGMON I, 2004, UNPUB
[3] Distribution of genes encoding resistance to streptogramin A and related compounds among staphylococci resistant to these antibiotics
Allignet, J
Aubert, S
Morvan, A
ElSolh, N
[J]. ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 1996, 40 (11) : 2523 - 2528
[4] Auerbach Tamar, 2002, Current Drug Targets - Infectious Disorders, V2, P169, DOI 10.2174/1568005023342506
[5] The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution
Ban, N
Nissen, P
Hansen, J
Moore, PB
Steitz, TA
[J]. SCIENCE, 2000, 289 (5481) : 905 - 920
[6] Ribosomal crystallography: Peptide bond formation and its inhibition
Bashan, A
Zarivach, R
Schluenzen, F
Agmon, I
Harms, J
Auerbach, T
Baram, D
Berisio, R
Bartels, H
Hansen, HAS
Fucini, P
Wilson, D
Peretz, M
Kessler, M
Yonath, A
[J]. BIOPOLYMERS, 2003, 70 (01) : 19 - 41
[7] Structural basis of the ribosomal machinery for peptide bond formation, translocation, and nascent chain progression
Bashan, A
Agmon, I
Zarivach, R
Schluenzen, F
Harms, J
Berisio, R
Bartels, H
Franceschi, F
Auerbach, T
Hansen, HAS
Kossoy, E
Kessler, M
Yonath, A
[J]. MOLECULAR CELL, 2003, 11 (01) : 91 - 102
[8] A conformational change in the ribosomal peptidyl transferase center upon active/inactive transition
Bayfield, MA
Dahlberg, AE
Schulmeister, U
Dorner, S
Barta, A
[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2001, 98 (18) : 10096 - 10101
[9] Structural insight into the antibiotic action of telithromycin against resistant mutants
Berisio, R
Harms, J
Schluenzen, F
Zarivach, R
Hansen, HAS
Fucini, P
Yonath, A
[J]. JOURNAL OF BACTERIOLOGY, 2003, 185 (14) : 4276 - 4279
[10] Structural insight into the role of the ribosomal tunnel in cellular regulation
Berisio, R
Schluenzen, F
Harms, J
Bashan, A
Auerbach, T
Baram, D
Yonath, A
[J]. NATURE STRUCTURAL BIOLOGY, 2003, 10 (05) : 366 - 370

← 1 2 3 4 5 6 →