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

Przemysław Grela; Michal J. Gajda; Jean Paul Armache; Roland Beckmann; Dawid Krokowski; Dmitri I. Svergun; Nikodem Grankowski; Marek Tchoŕzewski

doi:10.1042/BJ20120115

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

Przemysław Grela
, Michal J. Gajda
, Jean Paul Armache
, Roland Beckmann
, Dawid Krokowski
, Dmitri I. Svergun
, Nikodem Grankowski
, Marek Tchoŕzewski

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

11 Scopus citations

Abstract

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 five 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.

Original language	English (US)
Pages (from-to)	205-209
Number of pages	5
Journal	Biochemical Journal
Volume	444
Issue number	2
DOIs	https://doi.org/10.1042/BJ20120115
State	Published - Jun 1 2012

All Science Journal Classification (ASJC) codes

Biochemistry
Molecular Biology
Cell Biology

Access to Document

10.1042/BJ20120115

Cite this

@article{f61ef6ce86c84d25939da3346c649359,

title = "Solution structure of the natively assembled yeast ribosomal stalk etermined by small-angle X-ray scattering",

abstract = "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 five 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.",

author = "Przemys{\l}aw Grela and Gajda, \{Michal J.\} and Armache, \{Jean Paul\} and Roland Beckmann and Dawid Krokowski and Svergun, \{Dmitri I.\} and Nikodem Grankowski and Marek Tcho{\'r}zewski",

year = "2012",

month = jun,

day = "1",

doi = "10.1042/BJ20120115",

language = "English (US)",

volume = "444",

pages = "205--209",

journal = "Biochemical Journal",

issn = "0264-6021",

publisher = "Portland Press Ltd.",

number = "2",

}

TY - JOUR

T1 - Solution structure of the natively assembled yeast ribosomal stalk etermined by small-angle X-ray scattering

AU - Grela, Przemysław

AU - Gajda, Michal J.

AU - Armache, Jean Paul

AU - Beckmann, Roland

AU - Krokowski, Dawid

AU - Svergun, Dmitri I.

AU - Grankowski, Nikodem

AU - Tchoŕzewski, Marek

PY - 2012/6/1

Y1 - 2012/6/1

N2 - 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 five 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.

AB - 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 five 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.

UR - https://www.scopus.com/pages/publications/84860844975

UR - https://www.scopus.com/pages/publications/84860844975#tab=citedBy

U2 - 10.1042/BJ20120115

DO - 10.1042/BJ20120115

M3 - Article

C2 - 22458705

AN - SCOPUS:84860844975

SN - 0264-6021

VL - 444

SP - 205

EP - 209

JO - Biochemical Journal

JF - Biochemical Journal

IS - 2

ER -

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

Abstract

All Science Journal Classification (ASJC) codes

Access to Document

Other files and links

Fingerprint

Cite this