Ribosome crystallography: catalysis and evolution of peptide-bond formation., nascent chain elongation and its co-translational folding

被引：15

作者：

Bashan, A ^{[1
]}

Yonath, A ^{[1
]}

机构：

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

来源：

BIOCHEMICAL SOCIETY TRANSACTIONS | 2005年 / 33卷

关键词：

nascent chain elongation; peptide-bond formation; positional analysis; ribosome substrate-mediated catalysis; trigger factor;

D O I：

10.1042/BST0330488

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：

A ribosome is a ribozyme polymerizing amino acids, exploiting positional- and substrate-mediated chemical catalysis. We showed that peptide-bond formation is facilitated by the ribosomal architectural frame, provided by a sizable symmetry-related region in and around the peptidyl transferase centre, suggesting that the ribosomal active site was evolved by gene fusion. Mobility in tunnel components is exploited for elongation arrest as well as for trafficking nascent proteins into the folding space bordered by the bacterial chaperone, namely the trigger factor.

引用

页码：488 / 492

页数：5

共 33 条

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

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 .

FEBS LETTERS, 2004, 567 (01) :20-26

[2] 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 [J].

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 .

EUROPEAN JOURNAL OF BIOCHEMISTRY, 2003, 270 (12) :2543-2556

[3]

AGMON I, 2005, IN PRESS J MOL BIOL

[4] QUANTIFICATION OF TERTIARY STRUCTURAL CONSERVATION DESPITE PRIMARY SEQUENCE DRIFT IN THE GLOBIN FOLD [J].

ARONSON, HEG ;

ROYER, WE ;

HENDRICKSON, WA .

PROTEIN SCIENCE, 1994, 3 (10) :1706-1711

[5] The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution [J].

Ban, N ;

Nissen, P ;

Hansen, J ;

Moore, PB ;

Steitz, TA .

SCIENCE, 2000, 289 (5481) :905-920

[6] From peptide-bond formation to cotranslational folding: dynamic, regulatory and evolutionary aspects [J].

Baram, D ;

Yonath, A .

FEBS LETTERS, 2005, 579 (04) :948-954

[7]

Berg J M, 2001, Science, V291, P203

[8] Structural basis of the ribosomal machinery for peptide bond formation, translocation, and nascent chain progression [J].

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 .

MOLECULAR CELL, 2003, 11 (01) :91-102

[9]

BENSIO R, 2003, NAT STRUCT BIOL, V10, P366

[10] ENGINEERING ENZYME SPECIFICITY BY SUBSTRATE-ASSISTED CATALYSIS [J].

CARTER, P ;

WELLS, JA .

SCIENCE, 1987, 237 (4813) :394-399

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