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

Ilana Agmon; Maya Amit; Tamar Auerbach; Anat Bashan; David Baram; Heike Bartels; Rita Berisio; Inbal Greenberg; Joerg Harms; Harly A.S. Hansen; Maggie Kessler; Erez Pyetan; Frank Schluenzen; Assa Sittner; Ada Yonath; Raz Zarivach

doi:10.1016/j.febslet.2004.03.065

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

Ilana Agmon
, Maya Amit
, Tamar Auerbach
, Anat Bashan
, David Baram
, Heike Bartels
, Rita Berisio
, Inbal Greenberg
, Joerg Harms
, Harly A.S. Hansen
, Maggie Kessler
, Erez Pyetan
, Frank Schluenzen
, Assa Sittner
, Ada Yonath
, Raz Zarivach

Research output: Contribution to journal › Article › peer-review

36 Scopus citations

Abstract

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.

Original language	English
Pages (from-to)	20-26
Number of pages	7
Journal	FEBS Letters
Volume	567
Issue number	1
DOIs	https://doi.org/10.1016/j.febslet.2004.03.065
State	Published - 1 Jun 2004
Externally published	Yes

Keywords

Antibiotics synergism
Azithromycin
Dual binding
Peptide-bond formation
Positional catalysis
Ribosome
Synercid

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/j.febslet.2004.03.065

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Agmon, I., Amit, M., Auerbach, T., Bashan, A., Baram, D., Bartels, H., Berisio, R., Greenberg, I., Harms, J., Hansen, H. A. S., Kessler, M., Pyetan, E., Schluenzen, F., Sittner, A., Yonath, A., & Zarivach, R. (2004). Ribosomal crystallography: A flexible nucleotide anchoring tRNA translocation, facilitates peptide-bond formation, chirality discrimination and antibiotics synergism. FEBS Letters, 567(1), 20-26. https://doi.org/10.1016/j.febslet.2004.03.065

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abstract = "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.",

keywords = "Antibiotics synergism, Azithromycin, Dual binding, Peptide-bond formation, Positional catalysis, Ribosome, Synercid",

author = "Ilana Agmon and Maya Amit and Tamar Auerbach and Anat Bashan and David Baram and Heike Bartels and Rita Berisio and Inbal Greenberg and Joerg Harms and Hansen, \{Harly A.S.\} and Maggie Kessler and Erez Pyetan and Frank Schluenzen and Assa Sittner and Ada Yonath and Raz Zarivach",

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doi = "10.1016/j.febslet.2004.03.065",

language = "English",

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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 & Zarivach, R 2004, 'Ribosomal crystallography: A flexible nucleotide anchoring tRNA translocation, facilitates peptide-bond formation, chirality discrimination and antibiotics synergism', FEBS Letters, vol. 567, no. 1, pp. 20-26. https://doi.org/10.1016/j.febslet.2004.03.065

TY - JOUR

T1 - Ribosomal crystallography

T2 - A flexible nucleotide anchoring tRNA translocation, facilitates peptide-bond formation, chirality discrimination and antibiotics synergism

AU - Agmon, Ilana

AU - Amit, Maya

AU - Auerbach, Tamar

AU - Bashan, Anat

AU - Baram, David

AU - Bartels, Heike

AU - Berisio, Rita

AU - Greenberg, Inbal

AU - Harms, Joerg

AU - Hansen, Harly A.S.

AU - Kessler, Maggie

AU - Pyetan, Erez

AU - Schluenzen, Frank

AU - Sittner, Assa

AU - Yonath, Ada

AU - Zarivach, Raz

PY - 2004/6/1

Y1 - 2004/6/1

N2 - 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.

AB - 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.

KW - Antibiotics synergism

KW - Azithromycin

KW - Dual binding

KW - Peptide-bond formation

KW - Positional catalysis

KW - Ribosome

KW - Synercid

UR - https://www.scopus.com/pages/publications/2542445275

U2 - 10.1016/j.febslet.2004.03.065

DO - 10.1016/j.febslet.2004.03.065

M3 - Article

AN - SCOPUS:2542445275

SN - 0014-5793

VL - 567

SP - 20

EP - 26

JO - FEBS Letters

JF - FEBS Letters

IS - 1

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

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