Evidence map›Paper›PMID 16738137›Full record

ArticleNucleic acids research2006

New, extended hairpin form of the TAR-2 RNA domain points to the structural polymorphism at the 5' end of the HIV-2 leader RNA.

Katarzyna Pachulska-Wieczorek, Katarzyna J Purzycka, Ryszard W Adamiak

Abstract read
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Article in Nucleic acids research, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

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3 · Its place in the literature

Who cites it

10 citing papers in PubMed.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Katarzyna Pachulska-WieczorekLaboratory of Structural Chemistry of Nucleic Acids, Institute of Bioorganic Chemistry, Polish Academy of Sciences, Noskowskiego 12/14, 61-704 Poznań, Poland.
Katarzyna J Purzycka
Ryszard W Adamiak

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The HIV-2 TAR RNA domain (TAR-2) plays a key role in the trans-activation of HIV-2 transcription as it is the target for the Tat-2 protein and several cell factors. Here, we show that the TAR-2 domain exists in vitro in two global, alternative forms: a new, extended hairpin form with two conformers and the already proposed branched hairpins form. This points strongly to the structural polymorphism of the 5' end of the HIV-2 leader RNA. The evidence comes from the non-denaturing PAGE mobility assay, 2D structure prediction, enzymatic and Pb2+- or Mg2+-induced RNA cleavages. Existence of the TAR-2 extended form was further proved by the examination of engineered TAR-2 mutants stabilized either in the branched or extended structure. The TAR-2 extended form predominates with an increasing magnesium concentration. Gel retardation assays reveal that both TAR-2 wt and its mutant, unable to form branched structure, bind Tat-2 protein with comparable, high affinity, while RNA hairpins I and II, derived from TAR-2 branched structure model, show much less protein binding. We propose that an internal loop region of the TAR-2 extended hairpin form is a potential Tat-2 binding site.

Indexed as

HIV Long Terminal Repeat5' Untranslated RegionsArginineBase SequenceBinding SitesDiethyl PyrocarbonateElectrophoresis, Polyacrylamide GelElectrophoretic Mobility Shift AssayGene Products, tatHIV-2LeadMagnesiumMolecular Sequence DataNucleic Acid ConformationRibonucleasesRNA, Viral5' Untranslated RegionsargininamideArginineDiethyl PyrocarbonateGene Products, tatLeadMagnesiumRibonucleasesRNA, Viraltat Gene Products, Human Immunodeficiency Virus

Identifiers

PMID16738137
PMCPMC1474061

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.