The Structural Basis for mRNA Recognition and Cleavage by the Ribosome-Dependent Endonuclease ReIE

Cajetan Neubauer; Yong-Gui Gao; Kasper R. Andersen; Christine M. Dunham; Ann C. Kelley; Jendrik Hentschel; Kenn Gerdes; V. Ramakrishnan; Ditlev E. Brodersen

doi:10.1016/j.cell.2009.11.015

The Structural Basis for mRNA Recognition and Cleavage by the Ribosome-Dependent Endonuclease ReIE

Cajetan Neubauer, Yong-Gui Gao, Kasper R. Andersen, Christine M. Dunham, Ann C. Kelley, Jendrik Hentschel, Kenn Gerdes, V. Ramakrishnan, Ditlev E. Brodersen

147 Citationer (Scopus)

Abstract

Translational control is widely used to adjust gene expression levels. During the stringent response in bacteria, mRNA is degraded on the ribosome by the ribosome-dependent endonuclease, ReIE. The molecular basis for recognition of the ribosome and mRNA by ReIE and the mechanism of cleavage are unknown. Here, we present crystal structures of E. coli ReIE in isolation (2.5 angstrom) and bound to programmed Thermus thermophilus 70S ribosomes before (3.3 angstrom) and after (3.6 angstrom) cleavage. ReIE occupies the A site and causes cleavage of mRNA after the second nucleotide of the codon by reorienting and activating the mRNA for 2'-OH-induced hydrolysis. Stacking of A site codon bases with conserved residues in ReIE and 16S rRNA explains the requirement for the ribosome in catalysis and the subtle sequence specificity of the reaction. These structures provide detailed insight into the translational regulation on the bacterial ribosome by mRNA cleavage.

Originalsprog	Engelsk
Tidsskrift	Cell
Vol/bind	139
Udgave nummer	6
Sider (fra-til)	1084-1095
Antal sider	12
ISSN	0092-8674
DOI	https://doi.org/10.1016/j.cell.2009.11.015
Status	Udgivet - 2009
Udgivet eksternt	Ja

Adgang til dokumentet

10.1016/j.cell.2009.11.015

Citationsformater

@article{2af3f08353ff4716ab1ba267d8492323,

title = "The Structural Basis for mRNA Recognition and Cleavage by the Ribosome-Dependent Endonuclease ReIE",

abstract = "Translational control is widely used to adjust gene expression levels. During the stringent response in bacteria, mRNA is degraded on the ribosome by the ribosome-dependent endonuclease, ReIE. The molecular basis for recognition of the ribosome and mRNA by ReIE and the mechanism of cleavage are unknown. Here, we present crystal structures of E. coli ReIE in isolation (2.5 angstrom) and bound to programmed Thermus thermophilus 70S ribosomes before (3.3 angstrom) and after (3.6 angstrom) cleavage. ReIE occupies the A site and causes cleavage of mRNA after the second nucleotide of the codon by reorienting and activating the mRNA for 2'-OH-induced hydrolysis. Stacking of A site codon bases with conserved residues in ReIE and 16S rRNA explains the requirement for the ribosome in catalysis and the subtle sequence specificity of the reaction. These structures provide detailed insight into the translational regulation on the bacterial ribosome by mRNA cleavage.",

author = "Cajetan Neubauer and Yong-Gui Gao and Andersen, {Kasper R.} and Dunham, {Christine M.} and Kelley, {Ann C.} and Jendrik Hentschel and Kenn Gerdes and V. Ramakrishnan and Brodersen, {Ditlev E.}",

year = "2009",

doi = "10.1016/j.cell.2009.11.015",

language = "English",

volume = "139",

pages = "1084--1095",

journal = "Cell",

issn = "0092-8674",

publisher = "Cell Press",

number = "6",

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TY - JOUR

T1 - The Structural Basis for mRNA Recognition and Cleavage by the Ribosome-Dependent Endonuclease ReIE

AU - Neubauer, Cajetan

AU - Gao, Yong-Gui

AU - Andersen, Kasper R.

AU - Dunham, Christine M.

AU - Kelley, Ann C.

AU - Hentschel, Jendrik

AU - Gerdes, Kenn

AU - Ramakrishnan, V.

AU - Brodersen, Ditlev E.

PY - 2009

Y1 - 2009

N2 - Translational control is widely used to adjust gene expression levels. During the stringent response in bacteria, mRNA is degraded on the ribosome by the ribosome-dependent endonuclease, ReIE. The molecular basis for recognition of the ribosome and mRNA by ReIE and the mechanism of cleavage are unknown. Here, we present crystal structures of E. coli ReIE in isolation (2.5 angstrom) and bound to programmed Thermus thermophilus 70S ribosomes before (3.3 angstrom) and after (3.6 angstrom) cleavage. ReIE occupies the A site and causes cleavage of mRNA after the second nucleotide of the codon by reorienting and activating the mRNA for 2'-OH-induced hydrolysis. Stacking of A site codon bases with conserved residues in ReIE and 16S rRNA explains the requirement for the ribosome in catalysis and the subtle sequence specificity of the reaction. These structures provide detailed insight into the translational regulation on the bacterial ribosome by mRNA cleavage.

AB - Translational control is widely used to adjust gene expression levels. During the stringent response in bacteria, mRNA is degraded on the ribosome by the ribosome-dependent endonuclease, ReIE. The molecular basis for recognition of the ribosome and mRNA by ReIE and the mechanism of cleavage are unknown. Here, we present crystal structures of E. coli ReIE in isolation (2.5 angstrom) and bound to programmed Thermus thermophilus 70S ribosomes before (3.3 angstrom) and after (3.6 angstrom) cleavage. ReIE occupies the A site and causes cleavage of mRNA after the second nucleotide of the codon by reorienting and activating the mRNA for 2'-OH-induced hydrolysis. Stacking of A site codon bases with conserved residues in ReIE and 16S rRNA explains the requirement for the ribosome in catalysis and the subtle sequence specificity of the reaction. These structures provide detailed insight into the translational regulation on the bacterial ribosome by mRNA cleavage.

U2 - 10.1016/j.cell.2009.11.015

DO - 10.1016/j.cell.2009.11.015

M3 - Journal article

SN - 0092-8674

VL - 139

SP - 1084

EP - 1095

JO - Cell

JF - Cell

IS - 6

ER -