Structure of the HIV-1 Rev response element alone and in complex with regulator of virion (Rev) studied by atomic force microscopy

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Structure of the HIV-1 Rev response element alone and in complex with regulator of virion (Rev) studied by atomic force microscopy. / Pallesen, Jesper; Dong, Mingdong; Besenbacher, Flemming; Kjems, Jørgen.

I: F E B S Journal, Bind 276, Nr. 15, 2009, s. 4223-32.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

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@article{1c73d840726d11df8c1a000ea68e967b,
title = "Structure of the HIV-1 Rev response element alone and in complex with regulator of virion (Rev) studied by atomic force microscopy",
abstract = "The interaction of multiple HIV-1 regulator of virion (Rev) proteins with the viral RNA target, the Rev response element (RRE), is critical for nuclear export of incompletely spliced and unspliced viral RNA, and for the onset of the late phase in the viral replication cycle. The heterogeneity of the Rev-RRE complex has made it difficult to study using conventional structural methods. In the present study, atomic force microscopy is applied to directly visualize the tertiary structure of the RRE RNA alone and in complex with Rev proteins. The appearance of the RRE is compatible with the earlier proposed RRE secondary structure in dimensions and overall shape, including a stalk and a head interpreted as stem I, and stem-loops II-V in the secondary structure model, respectively. Atomic force microscopy imaging of the Rev-RRE complex revealed an increased height of the structure both in the stalk and head regions, which is in accordance with a binding model in which Rev binding to a high affinity site in stem IIB triggers oligomerization of Rev proteins through cooperative binding along stem I in RRE. The present study demonstrates that atomic force microscopy comprises a useful technique to study complex biological structures of nucleic acids at high resolution.",
keywords = "Base Sequence, Calorimetry, Genes, rev, HIV-1, Microscopy, Atomic Force, Molecular Sequence Data, Nucleic Acid Conformation, RNA, Viral, Thermodynamics, Virion, Virus Replication, rev Gene Products, Human Immunodeficiency Virus",
author = "Jesper Pallesen and Mingdong Dong and Flemming Besenbacher and J{\o}rgen Kjems",
year = "2009",
doi = "10.1111/j.1742-4658.2009.07130.x",
language = "English",
volume = "276",
pages = "4223--32",
journal = "F E B S Journal",
issn = "1742-464X",
publisher = "Wiley-Blackwell Publishing Ltd.",
number = "15",

}

RIS

TY - JOUR

T1 - Structure of the HIV-1 Rev response element alone and in complex with regulator of virion (Rev) studied by atomic force microscopy

AU - Pallesen, Jesper

AU - Dong, Mingdong

AU - Besenbacher, Flemming

AU - Kjems, Jørgen

PY - 2009

Y1 - 2009

N2 - The interaction of multiple HIV-1 regulator of virion (Rev) proteins with the viral RNA target, the Rev response element (RRE), is critical for nuclear export of incompletely spliced and unspliced viral RNA, and for the onset of the late phase in the viral replication cycle. The heterogeneity of the Rev-RRE complex has made it difficult to study using conventional structural methods. In the present study, atomic force microscopy is applied to directly visualize the tertiary structure of the RRE RNA alone and in complex with Rev proteins. The appearance of the RRE is compatible with the earlier proposed RRE secondary structure in dimensions and overall shape, including a stalk and a head interpreted as stem I, and stem-loops II-V in the secondary structure model, respectively. Atomic force microscopy imaging of the Rev-RRE complex revealed an increased height of the structure both in the stalk and head regions, which is in accordance with a binding model in which Rev binding to a high affinity site in stem IIB triggers oligomerization of Rev proteins through cooperative binding along stem I in RRE. The present study demonstrates that atomic force microscopy comprises a useful technique to study complex biological structures of nucleic acids at high resolution.

AB - The interaction of multiple HIV-1 regulator of virion (Rev) proteins with the viral RNA target, the Rev response element (RRE), is critical for nuclear export of incompletely spliced and unspliced viral RNA, and for the onset of the late phase in the viral replication cycle. The heterogeneity of the Rev-RRE complex has made it difficult to study using conventional structural methods. In the present study, atomic force microscopy is applied to directly visualize the tertiary structure of the RRE RNA alone and in complex with Rev proteins. The appearance of the RRE is compatible with the earlier proposed RRE secondary structure in dimensions and overall shape, including a stalk and a head interpreted as stem I, and stem-loops II-V in the secondary structure model, respectively. Atomic force microscopy imaging of the Rev-RRE complex revealed an increased height of the structure both in the stalk and head regions, which is in accordance with a binding model in which Rev binding to a high affinity site in stem IIB triggers oligomerization of Rev proteins through cooperative binding along stem I in RRE. The present study demonstrates that atomic force microscopy comprises a useful technique to study complex biological structures of nucleic acids at high resolution.

KW - Base Sequence

KW - Calorimetry

KW - Genes, rev

KW - HIV-1

KW - Microscopy, Atomic Force

KW - Molecular Sequence Data

KW - Nucleic Acid Conformation

KW - RNA, Viral

KW - Thermodynamics

KW - Virion

KW - Virus Replication

KW - rev Gene Products, Human Immunodeficiency Virus

U2 - 10.1111/j.1742-4658.2009.07130.x

DO - 10.1111/j.1742-4658.2009.07130.x

M3 - Journal article

C2 - 19583776

VL - 276

SP - 4223

EP - 4232

JO - F E B S Journal

JF - F E B S Journal

SN - 1742-464X

IS - 15

ER -