Bacterial polypeptide release factor RF2 is structurally distinct from eukaryotic eRF1

被引：156

作者：

Vestergaard, B

Van, LB

Andersen, GR

Nyborg, J

Buckingham, RH

Kjeldgaard, M ^{[1
]}

机构：

[1] Aarhus Univ, Inst Mol & Struct Biol, DK-8000 Aarhus C, Denmark

[2] CNRS, Inst Biol Physicochim, F-75005 Paris, France

来源：

MOLECULAR CELL | 2001年 / 8卷 / 06期

关键词：

D O I：

10.1016/S1097-2765(01)00415-4

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：

Bacterial release factor RF2 promotes termination of protein synthesis, specifically recognizing stop codons UAA or UGA. The crystal structure of Escherichia coli RF2 has been determined to a resolution of 1.8 Angstrom. RF2 is structurally distinct from its eukaryotic counterpart eRF1. The tripeptide SPF motif, thought to confer RF2 stop codon specificity, and the universally conserved GGQ motif, proposed to be involved with the peptidyl transferase center, are exposed in loops only 23 Angstrom apart, and the structure suggests that stop signal recognition is more complex than generally believed.

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页码：1375 / 1382

页数：8

相关论文

共 22 条

[1]

Arkov AL, 1999, BIOCHEMISTRY-MOSCOW+, V64, P1354

[2] Crystallography & NMR system:: A new software suite for macromolecular structure determination [J].

Brunger, AT ;

Adams, PD ;

Clore, GM ;

DeLano, WL ;

Gros, P ;

Grosse-Kunstleve, RW ;

Jiang, JS ;

Kuszewski, J ;

Nilges, M ;

Pannu, NS ;

Read, RJ ;

Rice, LM ;

Simonson, T ;

Warren, GL .

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 1998, 54 :905-921

[3] Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics [J].

Carter, AP ;

Clemons, WM ;

Brodersen, DE ;

Morgan-Warren, RJ ;

Wimberly, BT ;

Ramakrishnan, V .

NATURE, 2000, 407 (6802) :340-348

[4] The polypeptide chain release factor eRF1 specifically contacts the s4UGA stop codon located in the A site of eukaryotic ribosomes [J].

Chavatte, L ;

Frolova, L ;

Kisselev, L ;

Favre, A .

EUROPEAN JOURNAL OF BIOCHEMISTRY, 2001, 268 (10) :2896-2904

[5] THE CRYSTAL-STRUCTURE OF ELONGATION-FACTOR-G COMPLEXED WITH GDP, AT 2.7-ANGSTROM RESOLUTION [J].

CZWORKOWSKI, J ;

WANG, J ;

STEITZ, TA ;

MOORE, PB .

EMBO JOURNAL, 1994, 13 (16) :3661-3668

[6] A post-translational modification in the GGQ motif of RF2 from Escherichia coli stimulates termination of translation [J].

Dinçbas-Renqvist, V ;

Engström, Å ;

Mora, L ;

Heurgué-Hamard, V ;

Buckingham, R ;

Ehrenberg, M .

EMBO JOURNAL, 2000, 19 (24) :6900-6907

[7] Release factor RF3 in E-coli accelerates the dissociation of release factors RF1 and RF2 from the ribosome in a GTP-dependent manner [J].

Freistroffer, DV ;

Pavlov, MY ;

MacDougall, J ;

Buckingham, RH ;

Ehrenberg, M .

EMBO JOURNAL, 1997, 16 (13) :4126-4133

[8] Mutations in the highly conserved GGQ motif of class 1 polypeptide release factors abolish ability of human eRF1 to trigger peptidyl-tRNA hydrolysis [J].

Frolova, LY ;

Tsivkovskii, RY ;

Sivolobova, GF ;

Oparina, NY ;

Serpinsky, OI ;

Blinov, VM ;

Tatkov, SI ;

Kisselev, LL .

RNA, 1999, 5 (08) :1014-1020

[9] A tripeptide 'anticodon' deciphers stop codons in messenger RNA [J].

Ito, K ;

Uno, M ;

Nakamura, Y .

NATURE, 2000, 403 (6770) :680-684

[10] Conserved motifs in prokaryotic and eukaryotic polypeptide release factors: tRNA-protein mimicry hypothesis [J].

Ito, K ;

Ebihara, K ;

Uno, M ;

Nakamura, Y .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1996, 93 (11) :5443-5448