Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review
Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review
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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 -