skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: Crystal structures of complexes containing domains from two viral internal ribosome entry site (IRES) RNAs bound to the 70S ribosome

Abstract

Internal ribosome entry site (IRES) RNAs are elements of viral or cellular mRNAs that bypass steps of canonical eukaryotic cap-dependent translation initiation. Understanding of the structural basis of IRES mechanisms is limited, partially due to a lack of high-resolution structures of IRES RNAs bound to their cellular targets. Prompted by the universal phylogenetic conservation of the ribosomal P site, we solved the crystal structures of proposed P site binding domains from two intergenic region IRES RNAs bound to bacterial 70S ribosomes. The structures show that these IRES domains nearly perfectly mimic a tRNA-mRNA interaction. However, there are clear differences in the global shape and position of this IRES domain in the intersubunit space compared to those of tRNA, supporting a mechanism for IRES action that invokes hybrid state mimicry to drive a noncanonical mode of translocation. These structures suggest how relatively small structured RNAs can manipulate complex biological machines.

Authors:
; ; ; ; ;  [1];  [2]
  1. (UCSC)
  2. (
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
NSFNIH
OSTI Identifier:
1023038
Resource Type:
Journal Article
Journal Name:
Proc. Natl. Acad. Sci. USA
Additional Journal Information:
Journal Volume: 108; Journal Issue: (5) ; 02, 2011; Journal ID: ISSN 1091-6490
Country of Publication:
United States
Language:
ENGLISH
Subject:
59 BASIC BIOLOGICAL SCIENCES; 60 APPLIED LIFE SCIENCES; CRYSTAL STRUCTURE; RIBOSOMES; SHAPE; TARGETS; TRANSLOCATION

Citation Formats

Zhu, Jianyu, Korostelev, Andrei, Costantino, David A., Donohue, John P., Noller, Harry F., Kieft, Jeffrey S., and Colorado). Crystal structures of complexes containing domains from two viral internal ribosome entry site (IRES) RNAs bound to the 70S ribosome. United States: N. p., 2011. Web. doi:10.1073/pnas.1018582108.
Zhu, Jianyu, Korostelev, Andrei, Costantino, David A., Donohue, John P., Noller, Harry F., Kieft, Jeffrey S., & Colorado). Crystal structures of complexes containing domains from two viral internal ribosome entry site (IRES) RNAs bound to the 70S ribosome. United States. doi:10.1073/pnas.1018582108.
Zhu, Jianyu, Korostelev, Andrei, Costantino, David A., Donohue, John P., Noller, Harry F., Kieft, Jeffrey S., and Colorado). Wed . "Crystal structures of complexes containing domains from two viral internal ribosome entry site (IRES) RNAs bound to the 70S ribosome". United States. doi:10.1073/pnas.1018582108.
@article{osti_1023038,
title = {Crystal structures of complexes containing domains from two viral internal ribosome entry site (IRES) RNAs bound to the 70S ribosome},
author = {Zhu, Jianyu and Korostelev, Andrei and Costantino, David A. and Donohue, John P. and Noller, Harry F. and Kieft, Jeffrey S. and Colorado)},
abstractNote = {Internal ribosome entry site (IRES) RNAs are elements of viral or cellular mRNAs that bypass steps of canonical eukaryotic cap-dependent translation initiation. Understanding of the structural basis of IRES mechanisms is limited, partially due to a lack of high-resolution structures of IRES RNAs bound to their cellular targets. Prompted by the universal phylogenetic conservation of the ribosomal P site, we solved the crystal structures of proposed P site binding domains from two intergenic region IRES RNAs bound to bacterial 70S ribosomes. The structures show that these IRES domains nearly perfectly mimic a tRNA-mRNA interaction. However, there are clear differences in the global shape and position of this IRES domain in the intersubunit space compared to those of tRNA, supporting a mechanism for IRES action that invokes hybrid state mimicry to drive a noncanonical mode of translocation. These structures suggest how relatively small structured RNAs can manipulate complex biological machines.},
doi = {10.1073/pnas.1018582108},
journal = {Proc. Natl. Acad. Sci. USA},
issn = {1091-6490},
number = (5) ; 02, 2011,
volume = 108,
place = {United States},
year = {2011},
month = {8}
}