Solution structure of the natively assembled yeast ribosomal stalk determined by small-angle X-ray scattering

被引：11

作者：

Grela, Przemystaw ^{[1
]}

Gajda, Michal J. ^{[2
,3
]}

Armache, Jean-Paul ^{[4
]}

Beckmann, Roland ^{[4
]}

Krokowski, Dawid ^{[1
]}

Svergun, Dmitri I. ^{[2
]}

Grankowski, Nikodem ^{[1
]}

Tchorzewski, Marek ^{[1
]}

机构：

[1] Marie Curie Sklodowska Univ, Dept Mol Biol, PL-20033 Lublin, Poland

[2] Hamburg Outstn, European Mol Biol Lab, D-22603 Hamburg, Germany

[3] Max Planck Karl Bonhoeffer Inst Biophys Chem, D-37077 Gottingen, Germany

[4] Univ Munich, Dept Biochem, Gene Ctr, D-81377 Munich, Germany

来源：

BIOCHEMICAL JOURNAL | 2012年 / 444卷

关键词：

cryo-electron microscopy; GTPase centre; ribosomal P protein; ribosomal stalk; ribosome; small-angle X-ray scattering (SAXS); ELONGATION-FACTOR-G; C-TERMINAL DOMAIN; 80S RIBOSOME; SACCHAROMYCES-CEREVISIAE; ANGSTROM RESOLUTION; ESCHERICHIA-COLI; PROTEIN L12; GTPASE ACTIVATION; FACTOR-BINDING; CRYO-EM;

D O I：

10.1042/BJ20120115

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 ribosomal stalk of the 60S subunit has been shown to play a crucial role in all steps of protein synthesis, but its structure and exact molecular function remain an unanswered question. In the present study, we show the low-resolution models of the solution structure of the yeast ribosomal stalk, composed of live proteins, P0-(P1-P2)(2). The model of the pentameric stalk complex determined by small-angle X-ray scattering reveals an elongated shape with a maximum length of 13 nm. The model displays three distinct lobes, which may correspond to the individual P1-P2 heterodimers anchored to the C-terminal domain of the P0 protein.

引用

页码：205 / 209

页数：5

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