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Identification of the primary site of the human immunodeficiency virus type 1 RNA dimerization in vitro.
The results support a model in which dimer formation is initiated by the annealing of the palindromic sequences, possibly by a loop-loop interaction between the two monomers, and abolish dimerization, despite the presence of the previously postulated dimer linkage structure. Expand
Dimerization of retroviral RNA genomes: an inseparable pair
In this article, the current understanding of the relationship between retroviral genome conformation, dimerization and replication is reviewed. Expand
Functional sites in the 5' region of human immunodeficiency virus type 1 RNA form defined structural domains.
The conformation of the first 500 nucleotides covering the RNA leader and the 5' gag coding sequences of HIV-MAL, using chemical probing, shows the structural versatility of this region and suggests two mutually exclusive structures could modulate the different functions involving this domain. Expand
Modified nucleotides of tRNA(3Lys) modulate primer/template loop-loop interaction in the initiation complex of HIV-1 reverse transcription.
Sequence and structure comparisons indicate that the primer/template loop-loop interaction is conserved in all HIV-1 isolates, and possibly also in HIV-2 and SIV. Expand
A loop-loop "kissing" complex is the essential part of the dimer linkage of genomic HIV-1 RNA.
It is shown that in vitro dimerization of HIV-1 RNA is a specific process, not resulting from simple annealing of denatured molecules, and that 55-mer sense RNAs containing the DIS are able to interfere with the preformed HIV- 1 RNA dimer. Expand
Initiation of reverse transcription of HIV-1: secondary structure of the HIV-1 RNA/tRNA(3Lys) (template/primer).
An unexpectedly complex and compact pseudoknot-like structure in which most of the anticodon loop, the 3' strand ofThe anticodon stem and the 5' part of the variable loop of tRNA(3Lys) interact with viral sequences 12 to 39 nucleotides upstream of the PBS is revealed. Expand
Mutational analysis of the bipartite dimer linkage structure of human immunodeficiency virus type 1 genomic RNA.
It is shown that single base mutations in the palindromic loop of the dimerization initiation site completely abolish Dimerization, while introduction of compensatory mutations restores the process. Expand
Specific recognition of the HIV-1 genomic RNA by the Gag precursor.
By using RNA binding and footprinting assays, it is demonstrated that the primary Pr55(Gag) binding site on the gRNA consists of the internal loop and the lower part of stem-loop 1 (SL1), the upper part of which initiates gRNA dimerization. Expand
Dimerization of human immunodeficiency virus (type 1) RNA: stimulation by cations and possible mechanism.
Results indicate that all in vitro generated HIV-1 RNAs containing a 100 nucleotide domain downstream from the 5' splice site are able to dimerize, and a consensus sequence PuGGAPuA found in the putative dimerization-encapsidation region of all retroviral genomes examined may participate in theDimerization process. Expand
A supramolecular assembly formed by influenza A virus genomic RNA segments
The influenza A virus genome consists of eight viral RNAs (vRNAs) that form viral ribonucleoproteins (vRNPs). Even though evidence supporting segment-specific packaging of vRNAs is accumulating, theExpand