Role of the trans-activation response element in dimerization of HIV-1 RNA

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Role of the trans-activation response element in dimerization of HIV-1 RNA. / Andersen, Ebbe S; Contera, Sonia Antoranz; Knudsen, Bjarne; Damgaard, Christian K; Besenbacher, Flemming; Kjems, Jørgen.

In: Journal of Biological Chemistry, Vol. 279, No. 21, 21.05.2004, p. 22243-22249.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

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Andersen, Ebbe S ; Contera, Sonia Antoranz ; Knudsen, Bjarne ; Damgaard, Christian K ; Besenbacher, Flemming ; Kjems, Jørgen. / Role of the trans-activation response element in dimerization of HIV-1 RNA. In: Journal of Biological Chemistry. 2004 ; Vol. 279, No. 21. pp. 22243-22249.

Bibtex

@article{1f2b000071a64ba6a2257040b8a91a26,
title = "Role of the trans-activation response element in dimerization of HIV-1 RNA",
abstract = "The HIV-1 genome consists of two identical RNA strands that are linked together through non-covalent interactions. A major determinant for efficient dimerization of the two RNA strands is the interaction between palindromic sequences in the dimerization initiation site. Here we use an interplay of bioinformatics, biochemistry, and atomic force microscopy to describe another conserved palindrome in the trans-activation response element (TAR) that functions as a strong dimerization site when transiently exposed to the viral nucleocapsid protein. In conjunction with the DIS interaction, the TAR dimerization induces the formation of a 65-nm higher-order circular structure in the dimeric HIV-1 RNA. Our results provide a molecular model for the role of TAR in packaging and reverse transcription of the viral genome. The unique structure of the TAR-TAR dimer renders it an intriguing therapeutic target for the treatment of HIV-1 infection.",
keywords = "5' Untranslated Regions, Base Sequence, Dimerization, HIV-1, Microscopy, Atomic Force, Molecular Sequence Data, Nucleic Acid Conformation, Nucleocapsid, Phylogeny, Plasmids, Protein Binding, RNA, Viral, Response Elements, Time Factors, Transcription, Genetic, Transcriptional Activation",
author = "Andersen, {Ebbe S} and Contera, {Sonia Antoranz} and Bjarne Knudsen and Damgaard, {Christian K} and Flemming Besenbacher and J{\o}rgen Kjems",
year = "2004",
month = "5",
day = "21",
doi = "10.1074/jbc.M314326200",
language = "English",
volume = "279",
pages = "22243--22249",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "21",

}

RIS

TY - JOUR

T1 - Role of the trans-activation response element in dimerization of HIV-1 RNA

AU - Andersen, Ebbe S

AU - Contera, Sonia Antoranz

AU - Knudsen, Bjarne

AU - Damgaard, Christian K

AU - Besenbacher, Flemming

AU - Kjems, Jørgen

PY - 2004/5/21

Y1 - 2004/5/21

N2 - The HIV-1 genome consists of two identical RNA strands that are linked together through non-covalent interactions. A major determinant for efficient dimerization of the two RNA strands is the interaction between palindromic sequences in the dimerization initiation site. Here we use an interplay of bioinformatics, biochemistry, and atomic force microscopy to describe another conserved palindrome in the trans-activation response element (TAR) that functions as a strong dimerization site when transiently exposed to the viral nucleocapsid protein. In conjunction with the DIS interaction, the TAR dimerization induces the formation of a 65-nm higher-order circular structure in the dimeric HIV-1 RNA. Our results provide a molecular model for the role of TAR in packaging and reverse transcription of the viral genome. The unique structure of the TAR-TAR dimer renders it an intriguing therapeutic target for the treatment of HIV-1 infection.

AB - The HIV-1 genome consists of two identical RNA strands that are linked together through non-covalent interactions. A major determinant for efficient dimerization of the two RNA strands is the interaction between palindromic sequences in the dimerization initiation site. Here we use an interplay of bioinformatics, biochemistry, and atomic force microscopy to describe another conserved palindrome in the trans-activation response element (TAR) that functions as a strong dimerization site when transiently exposed to the viral nucleocapsid protein. In conjunction with the DIS interaction, the TAR dimerization induces the formation of a 65-nm higher-order circular structure in the dimeric HIV-1 RNA. Our results provide a molecular model for the role of TAR in packaging and reverse transcription of the viral genome. The unique structure of the TAR-TAR dimer renders it an intriguing therapeutic target for the treatment of HIV-1 infection.

KW - 5' Untranslated Regions

KW - Base Sequence

KW - Dimerization

KW - HIV-1

KW - Microscopy, Atomic Force

KW - Molecular Sequence Data

KW - Nucleic Acid Conformation

KW - Nucleocapsid

KW - Phylogeny

KW - Plasmids

KW - Protein Binding

KW - RNA, Viral

KW - Response Elements

KW - Time Factors

KW - Transcription, Genetic

KW - Transcriptional Activation

U2 - 10.1074/jbc.M314326200

DO - 10.1074/jbc.M314326200

M3 - Journal article

C2 - 15014074

VL - 279

SP - 22243

EP - 22249

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 21

ER -