From peptide-bond formation to cotranslational folding: dynamic, regulatory and evolutionary aspects

被引：40

作者：

Baram, D ^{[1
]}

Yonath, A ^{[1
]}

机构：

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

来源：

FEBS LETTERS | 2005年 / 579卷 / 04期

关键词：

ribosomal catalysis; antibiotics selectivity; ribosome evolution; trigger factor; ribosome-recycling factor;

D O I：

10.1016/j.febslet.2004.11.063

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：

Ribosomes are ribozymes exerting substrate positioning and promoting substrate-mediated catalysis. Peptide-bonds are formed within a symmetrical region, thus suggesting that ribosomes evolved by gene-fusion. Remote interactions dominate substrate positioning at stereochemistry suitable for peptide-bond formation and elaborate architectural-design guides the processivity of the reaction by rotatory motion. Nascent proteins are directed into the exit tunnel at extended conformation, complying with the tunnel's narrow entrance. Tunnel dynamics facilitate its interactive participation in elongation, discrimination, cellular signaling and nascent-protein trafficking into the chaperon-aided folding site. Conformational alterations, induced by ribosomal-recycling factor, facilitate subunit dissociation. Remarkably, although antibiotics discrimination is determined by the identity of a single nucleotide, involved also in resistance, additional nucleotides dictate antibiotics effectiveness. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights resevered.

引用

页码：948 / 954

页数：7

共 51 条

[11] Activity of telithromycin compared with seven other agents against 1039 Streptococcus pyogenes pediatric isolates from ten centers in central and eastern Europe [J].

Bozdogan, B ;

Appelbaum, PC ;

Kelly, LM ;

Hoellman, DB ;

Tambic-Andrasevic, A ;

Drukalska, L ;

Hryniewicz, W ;

Hupkova, H ;

Jacobs, MR ;

Kolman, J ;

Konkoly-Thege, M ;

Miciuleviciene, J ;

Pana, M ;

Setchanova, L ;

Trupl, J ;

Urbaskova, P .

CLINICAL MICROBIOLOGY AND INFECTION, 2003, 9 (07) :741-745

[12] Histidine 229 in protein L2 is apparently essential for 50S peptidyl transferase activity [J].

Cooperman, BS ;

Wooten, T ;

Romero, DP ;

Traut, RR .

BIOCHEMISTRY AND CELL BIOLOGY, 1995, 73 (11-12) :1087-1094

[13] L22 ribosomal protein and effect of its mutation on ribosome resistance to erythromycin [J].

Davydova, N ;

Streltsov, V ;

Wilce, M ;

Liljas, A ;

Garber, M .

JOURNAL OF MOLECULAR BIOLOGY, 2002, 322 (03) :635-644

[14] Molecular aspects of the ribosomal peptidyl transferase [J].

Dorner, S ;

Polacek, N ;

Schulmeister, U ;

Panuschka, C ;

Barta, A .

BIOCHEMICAL SOCIETY TRANSACTIONS, 2002, 30 :1131-1137

[15]

EISENSTEIN M, 1994, SUPRAMOLECULAR STRUC, V4, P213

[16] The dynamic tunnel [J].

Etchells, SA ;

Hartl, FU .

NATURE STRUCTURAL & MOLECULAR BIOLOGY, 2004, 11 (05) :391-392

[17] Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins [J].

Ferbitz, L ;

Maier, T ;

Patzelt, H ;

Bukau, B ;

Deuerling, E ;

Ban, N .

NATURE, 2004, 431 (7008) :590-596

[18] Folding of newly translated proteins in vivo: The role of molecular chaperones [J].

Frydman, J .

ANNUAL REVIEW OF BIOCHEMISTRY, 2001, 70 :603-647

[19] The polypeptide tunnel system in the ribosome and its gating in erythromycin resistance mutants of L4 and L22 [J].

Gabashvili, IS ;

Gregory, ST ;

Valle, M ;

Grassucci, R ;

Worbs, M ;

Wahl, MC ;

Dahlberg, AE ;

Frank, J .

MOLECULAR CELL, 2001, 8 (01) :181-188

[20] Three-dimensional structures of translating ribosomes by cryo-EM [J].

Gilbert, RJC ;

Fucini, P ;

Connell, S ;

Fuller, SD ;

Nierhaus, KH ;

Robinson, CV ;

Dobson, CM ;

Stuart, DI .

MOLECULAR CELL, 2004, 14 (01) :57-66

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