Functional characterization of IRESes by an inhibitor of the RNA helicase eIF4A

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Functional characterization of IRESes by an inhibitor of the RNA helicase eIF4A. / Bordeleau, Marie-Eve; Mori, Ayaka; Oberer, Monika; Lindqvist, Lisa; Chard, Louisa S; Higa, Tatsuo; Belsham, Graham J; Wagner, Gerhard; Tanaka, Junichi; Pelletier, Jerry.

In: Nature Chemical Biology, Vol. 2, No. 4, 04.2006, p. 213-20.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Bordeleau, M-E, Mori, A, Oberer, M, Lindqvist, L, Chard, LS, Higa, T, Belsham, GJ, Wagner, G, Tanaka, J & Pelletier, J 2006, 'Functional characterization of IRESes by an inhibitor of the RNA helicase eIF4A', Nature Chemical Biology, vol. 2, no. 4, pp. 213-20. https://doi.org/10.1038/nchembio776

APA

Bordeleau, M-E., Mori, A., Oberer, M., Lindqvist, L., Chard, L. S., Higa, T., Belsham, G. J., Wagner, G., Tanaka, J., & Pelletier, J. (2006). Functional characterization of IRESes by an inhibitor of the RNA helicase eIF4A. Nature Chemical Biology, 2(4), 213-20. https://doi.org/10.1038/nchembio776

Vancouver

Bordeleau M-E, Mori A, Oberer M, Lindqvist L, Chard LS, Higa T et al. Functional characterization of IRESes by an inhibitor of the RNA helicase eIF4A. Nature Chemical Biology. 2006 Apr;2(4):213-20. https://doi.org/10.1038/nchembio776

Author

Bordeleau, Marie-Eve ; Mori, Ayaka ; Oberer, Monika ; Lindqvist, Lisa ; Chard, Louisa S ; Higa, Tatsuo ; Belsham, Graham J ; Wagner, Gerhard ; Tanaka, Junichi ; Pelletier, Jerry. / Functional characterization of IRESes by an inhibitor of the RNA helicase eIF4A. In: Nature Chemical Biology. 2006 ; Vol. 2, No. 4. pp. 213-20.

Bibtex

@article{8e3996c4fbc14329a053e2471e34a64d,
title = "Functional characterization of IRESes by an inhibitor of the RNA helicase eIF4A",
abstract = "RNA helicases are molecular motors that are involved in virtually all aspects of RNA metabolism. Eukaryotic initiation factor (eIF) 4A is the prototypical member of the DEAD-box family of RNA helicases. It is thought to use energy from ATP hydrolysis to unwind mRNA structure and, in conjunction with other translation factors, it prepares mRNA templates for ribosome recruitment during translation initiation. In screening marine extracts for new eukaryotic translation initiation inhibitors, we identified the natural product hippuristanol. We show here that this compound is a selective and potent inhibitor of eIF4A RNA-binding activity that can be used to distinguish between eIF4A-dependent and -independent modes of translation initiation in vitro and in vivo. We also show that poliovirus replication is delayed when infected cells are exposed to hippuristanol. Our study demonstrates the feasibility of selectively targeting members of the DEAD-box helicase family with small-molecule inhibitors.",
keywords = "Adenosine Triphosphate/chemistry, Cross-Linking Reagents/chemistry, Dose-Response Relationship, Drug, Escherichia coli/metabolism, Eukaryotic Initiation Factor-4A/chemistry, Humans, Hydrolysis, Magnetic Resonance Spectroscopy, Models, Genetic, Plasmids/metabolism, Poliovirus/genetics, Promoter Regions, Genetic, Protein Binding, Protein Biosynthesis, RNA/chemistry, RNA Helicases/chemistry, RNA, Messenger/metabolism, Recombinant Proteins/chemistry, Ribosomes/chemistry, Structure-Activity Relationship, Transfection",
author = "Marie-Eve Bordeleau and Ayaka Mori and Monika Oberer and Lisa Lindqvist and Chard, {Louisa S} and Tatsuo Higa and Belsham, {Graham J} and Gerhard Wagner and Junichi Tanaka and Jerry Pelletier",
year = "2006",
month = apr,
doi = "10.1038/nchembio776",
language = "English",
volume = "2",
pages = "213--20",
journal = "Nature Chemical Biology",
issn = "1552-4450",
publisher = "nature publishing group",
number = "4",

}

RIS

TY - JOUR

T1 - Functional characterization of IRESes by an inhibitor of the RNA helicase eIF4A

AU - Bordeleau, Marie-Eve

AU - Mori, Ayaka

AU - Oberer, Monika

AU - Lindqvist, Lisa

AU - Chard, Louisa S

AU - Higa, Tatsuo

AU - Belsham, Graham J

AU - Wagner, Gerhard

AU - Tanaka, Junichi

AU - Pelletier, Jerry

PY - 2006/4

Y1 - 2006/4

N2 - RNA helicases are molecular motors that are involved in virtually all aspects of RNA metabolism. Eukaryotic initiation factor (eIF) 4A is the prototypical member of the DEAD-box family of RNA helicases. It is thought to use energy from ATP hydrolysis to unwind mRNA structure and, in conjunction with other translation factors, it prepares mRNA templates for ribosome recruitment during translation initiation. In screening marine extracts for new eukaryotic translation initiation inhibitors, we identified the natural product hippuristanol. We show here that this compound is a selective and potent inhibitor of eIF4A RNA-binding activity that can be used to distinguish between eIF4A-dependent and -independent modes of translation initiation in vitro and in vivo. We also show that poliovirus replication is delayed when infected cells are exposed to hippuristanol. Our study demonstrates the feasibility of selectively targeting members of the DEAD-box helicase family with small-molecule inhibitors.

AB - RNA helicases are molecular motors that are involved in virtually all aspects of RNA metabolism. Eukaryotic initiation factor (eIF) 4A is the prototypical member of the DEAD-box family of RNA helicases. It is thought to use energy from ATP hydrolysis to unwind mRNA structure and, in conjunction with other translation factors, it prepares mRNA templates for ribosome recruitment during translation initiation. In screening marine extracts for new eukaryotic translation initiation inhibitors, we identified the natural product hippuristanol. We show here that this compound is a selective and potent inhibitor of eIF4A RNA-binding activity that can be used to distinguish between eIF4A-dependent and -independent modes of translation initiation in vitro and in vivo. We also show that poliovirus replication is delayed when infected cells are exposed to hippuristanol. Our study demonstrates the feasibility of selectively targeting members of the DEAD-box helicase family with small-molecule inhibitors.

KW - Adenosine Triphosphate/chemistry

KW - Cross-Linking Reagents/chemistry

KW - Dose-Response Relationship, Drug

KW - Escherichia coli/metabolism

KW - Eukaryotic Initiation Factor-4A/chemistry

KW - Humans

KW - Hydrolysis

KW - Magnetic Resonance Spectroscopy

KW - Models, Genetic

KW - Plasmids/metabolism

KW - Poliovirus/genetics

KW - Promoter Regions, Genetic

KW - Protein Binding

KW - Protein Biosynthesis

KW - RNA/chemistry

KW - RNA Helicases/chemistry

KW - RNA, Messenger/metabolism

KW - Recombinant Proteins/chemistry

KW - Ribosomes/chemistry

KW - Structure-Activity Relationship

KW - Transfection

U2 - 10.1038/nchembio776

DO - 10.1038/nchembio776

M3 - Journal article

C2 - 16532013

VL - 2

SP - 213

EP - 220

JO - Nature Chemical Biology

JF - Nature Chemical Biology

SN - 1552-4450

IS - 4

ER -

ID: 257919071