Evidence map›Paper›PMID 19449839›Full record

ArticleBiochemistry2009

Probing anomalous structural features in polypurine tract-containing RNA-DNA hybrids with neomycin B.

Robert G Brinson, Kevin B Turner, Hye Young Yi-Brunozzi, Stuart F J Le Grice, Daniele Fabris, John P Marino

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.8field-weighted citation impact, top 29% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

9 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Targeting the HIV RNA genome: high-hanging fruit only needs a longer ladder.Current topics in microbiology and immunology · 2015
    Review
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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

6 authors at 4 institutions in 1 country.

Robert G BrinsonCenter for Advanced Research in Biotechnology of the University of Maryland Biotechnology Institute and the National Institute of Standards and Technology, 9600 Gudelsky Drive, Rockville, Maryland 20850, USA.
Kevin B Turner
Hye Young Yi-Brunozzi
Stuart F J Le Grice
Daniele Fabris
John P Marino
National Institutes of Health · USUniversity of Maryland, Baltimore County · USNational Cancer Institute · USNational Institute of Standards and Technology · US

Funding

Nucleic Acid Footprinting and development of small molecule antagonistsZIABC010493 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI LE GRICE, STUART F. J. · 2009 to 2021
$9.3M
STRUCTURAL BASIS OF RNA STEM LOOP KISSING INTERACTIONSR01GM059107 · NIGMS · UNIVERSITY OF MD BIOTECHNOLOGY INSTITUTE · PI MARINO, JOHN PAUL · 1999 to 2008
$1.7M
Intramural NIH HHSNIGMS NIH HHS GM59107NIGMS NIH HHS GM643208NIGMS NIH HHS R01 GM059107
6 · The paper itself

Abstract

During (-)-strand DNA synthesis in retroviruses and Saccharomyces cerevisiae LTR retrotransposons, a purine rich region of the RNA template, known as the polypurine tract (PPT), is resistant to RNase H-mediated hydrolysis and subsequently serves as a primer for (+)-strand, DNA-dependent DNA synthesis. Although HIV-1 and Ty3 PPT sequences share no sequence similarity beyond the fact that both include runs of purine ribonucleotides, it has been suggested that these PPTs are processed by their cognate reverse transcriptases (RTs) through a common molecular mechanism. Here, we have used the aminoglycoside neomycin B (NB) to examine which structural features of the Ty3 PPT contribute to specific recognition and processing by its cognate RT. Using high-resolution NMR, direct infusion FTICR mass spectrometry, and isothermal titration calorimetry, we show that NB binds preferentially and selectively adjacent to the Ty3 3' PPT-U3 cleavage junction and in an upstream 5' region where the thumb subdomain of Ty3 RT putatively grips the substrate. Regions highlighted by NB on the Ty3 PPT are similar to those previously identified on the HIV-1 PPT sequence that are implicated as contact points for substrate binding by its RT. Our findings thus support the notion that common structural features of lentiviral and LTR-retrotransposon PPTs facilitate the interaction with their cognate RT.

Indexed as

Molecular ProbesBase SequenceCalorimetryDNAFramycetinMass SpectrometryNuclear Magnetic Resonance, BiomolecularNucleic Acid HybridizationPurinesRNASpectroscopy, Fourier Transform InfraredDNAFramycetinMolecular ProbesPurinesRNA

Identifiers

PMID19449839
PMCPMC2802280
OpenAlexW1994261851

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.