A time-resolved investigation of ribosomal subunit association

Scott P. Hennelly; Ayman Antoun; Måns Ehrenberg; Claudio O. Gualerzi; William Knight; J. Stephen Lodmell; Walter E. Hill

doi:10.1016/j.jmb.2004.12.054

A time-resolved investigation of ribosomal subunit association

Scott P. Hennelly, Ayman Antoun, Måns Ehrenberg, Claudio O. Gualerzi, William Knight, J. Stephen Lodmell, Walter E. Hill

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

48 Scopus citations

Abstract

The notion that the ribosome is dynamic has been supported by various biochemical techniques, as well as by differences observed in high-resolution structures of ribosomal complexes frozen in various functional states. Yet, the mechanisms and extent of rRNA dynamics are still largely unknown. We have used a novel, fast chemical-modification technique to provide time-resolved details of 16 S rRNA structural changes that occur as bridges are formed between the ribosomal subunits as they associate. Association of different 16 S rRNA regions was found to be a sequential, multi-step process involving conformational rearrangements within the 30 S subunit. Our results suggest that key regions of 16 S rRNA, necessary for decoding and tRNA A-site binding, are structurally altered in a time-dependent manner by association with the 50 S ribosomal subunits.

Original language	English
Pages (from-to)	1243-1258
Number of pages	16
Journal	Journal of Molecular Biology
Volume	346
Issue number	5
DOIs	https://doi.org/10.1016/j.jmb.2004.12.054
State	Published - Mar 11 2005

Keywords

Dynamics
RNA
Ribosome
Structure
Subunit association

Access to Document

10.1016/j.jmb.2004.12.054

Cite this

@article{1d76318c5815435a9a7be71b63088e80,

title = "A time-resolved investigation of ribosomal subunit association",

abstract = "The notion that the ribosome is dynamic has been supported by various biochemical techniques, as well as by differences observed in high-resolution structures of ribosomal complexes frozen in various functional states. Yet, the mechanisms and extent of rRNA dynamics are still largely unknown. We have used a novel, fast chemical-modification technique to provide time-resolved details of 16 S rRNA structural changes that occur as bridges are formed between the ribosomal subunits as they associate. Association of different 16 S rRNA regions was found to be a sequential, multi-step process involving conformational rearrangements within the 30 S subunit. Our results suggest that key regions of 16 S rRNA, necessary for decoding and tRNA A-site binding, are structurally altered in a time-dependent manner by association with the 50 S ribosomal subunits.",

keywords = "Dynamics, RNA, Ribosome, Structure, Subunit association",

author = "Hennelly, {Scott P.} and Ayman Antoun and M{\aa}ns Ehrenberg and Gualerzi, {Claudio O.} and William Knight and Lodmell, {J. Stephen} and Hill, {Walter E.}",

note = "Funding Information: We thank the following good people for technical support and insightful conversation: Marty Rice, Bill Bowen, Jean-Marc Lanchy, Chuck Merryman, Attilio Fabretti and Stefano Marzi. This work has been supported, in part, by NIH grant GM 35717 (to W.E.H.), Swedish Research Council grant (to M.E.) and Egyptian Mission Department grant (to A.A.), and grants MIUR-PRIN 2003 and EC-“Ribosome Inhibitors” (to C.O.G.).",

year = "2005",

month = mar,

day = "11",

doi = "10.1016/j.jmb.2004.12.054",

language = "English",

volume = "346",

pages = "1243--1258",

journal = "Journal of Molecular Biology",

issn = "0022-2836",

publisher = "Academic Press",

number = "5",

}

TY - JOUR

T1 - A time-resolved investigation of ribosomal subunit association

AU - Hennelly, Scott P.

AU - Antoun, Ayman

AU - Ehrenberg, Måns

AU - Gualerzi, Claudio O.

AU - Knight, William

AU - Lodmell, J. Stephen

AU - Hill, Walter E.

N1 - Funding Information: We thank the following good people for technical support and insightful conversation: Marty Rice, Bill Bowen, Jean-Marc Lanchy, Chuck Merryman, Attilio Fabretti and Stefano Marzi. This work has been supported, in part, by NIH grant GM 35717 (to W.E.H.), Swedish Research Council grant (to M.E.) and Egyptian Mission Department grant (to A.A.), and grants MIUR-PRIN 2003 and EC-“Ribosome Inhibitors” (to C.O.G.).

PY - 2005/3/11

Y1 - 2005/3/11

N2 - The notion that the ribosome is dynamic has been supported by various biochemical techniques, as well as by differences observed in high-resolution structures of ribosomal complexes frozen in various functional states. Yet, the mechanisms and extent of rRNA dynamics are still largely unknown. We have used a novel, fast chemical-modification technique to provide time-resolved details of 16 S rRNA structural changes that occur as bridges are formed between the ribosomal subunits as they associate. Association of different 16 S rRNA regions was found to be a sequential, multi-step process involving conformational rearrangements within the 30 S subunit. Our results suggest that key regions of 16 S rRNA, necessary for decoding and tRNA A-site binding, are structurally altered in a time-dependent manner by association with the 50 S ribosomal subunits.

AB - The notion that the ribosome is dynamic has been supported by various biochemical techniques, as well as by differences observed in high-resolution structures of ribosomal complexes frozen in various functional states. Yet, the mechanisms and extent of rRNA dynamics are still largely unknown. We have used a novel, fast chemical-modification technique to provide time-resolved details of 16 S rRNA structural changes that occur as bridges are formed between the ribosomal subunits as they associate. Association of different 16 S rRNA regions was found to be a sequential, multi-step process involving conformational rearrangements within the 30 S subunit. Our results suggest that key regions of 16 S rRNA, necessary for decoding and tRNA A-site binding, are structurally altered in a time-dependent manner by association with the 50 S ribosomal subunits.

KW - Dynamics

KW - RNA

KW - Ribosome

KW - Structure

KW - Subunit association

UR - http://www.scopus.com/inward/record.url?scp=13844280352&partnerID=8YFLogxK

U2 - 10.1016/j.jmb.2004.12.054

DO - 10.1016/j.jmb.2004.12.054

M3 - Article

C2 - 15713478

AN - SCOPUS:13844280352

SN - 0022-2836

VL - 346

SP - 1243

EP - 1258

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

IS - 5

ER -

A time-resolved investigation of ribosomal subunit association

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Cite this