Evidence map›Paper›PMID 26673717›Full record

ArticleNucleic acids research2016

L1 retrotransposition requires rapid ORF1p oligomerization, a novel coiled coil-dependent property conserved despite extensive remodeling.

M Nabuan Naufer, Kathryn E Callahan, Pamela R Cook, Cesar E Perez-Gonzalez, Mark C Williams, Anthony V Furano

Abstract read
In one paragraph

Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
–field-weighted citation impact
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

27 citing papers in PubMed.

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  15. Article
  16. L1 retrotransposons exploit RNA mNature communications · 2021
    Article
  17. Article
  18. Article
  19. Article
  20. Protein-nucleic acid interactions of LINE-1 ORF1p.Seminars in cell & developmental biology · 2019
    Review
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.

M Nabuan NauferNortheastern University, Department of Physics, Boston, MA 02115, USA.
Kathryn E CallahanLaboratory of Cellular and Molecular Biology, NIDDK, National Institutes of Health, Bethesda, MD 20892, USA.
Pamela R CookLaboratory of Cellular and Molecular Biology, NIDDK, National Institutes of Health, Bethesda, MD 20892, USA.
Cesar E Perez-GonzalezLaboratory of Cellular and Molecular Biology, NIDDK, National Institutes of Health, Bethesda, MD 20892, USA.
Mark C WilliamsNortheastern University, Department of Physics, Boston, MA 02115, USA mark@neu.edu.
Anthony V FuranoLaboratory of Cellular and Molecular Biology, NIDDK, National Institutes of Health, Bethesda, MD 20892, USA avf@helix.nih.gov.

Funding

Mammalian L1 retrotransposon replicationZIADK057601 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI FURANO, ANTHONY V. · 2009 to 2022
$7.2M
Single Molecule HIV-1 Replication InteractionsR01GM072462 · NIGMS · NORTHEASTERN UNIVERSITY · PI WILLIAMS, MARK C · 2004 to 2018
$3.9M
Intramural NIH HHSNIGMS NIH HHS R01 GM072462NIGMS NIH HHS R01GM072462PHS HHS HNK6H7
6 · The paper itself

Abstract

Detailed mechanistic understanding of L1 retrotransposition is sparse, particularly with respect to ORF1p, a coiled coil-mediated homotrimeric nucleic acid chaperone that can form tightly packed oligomers on nucleic acids. Although the coiled coil motif is highly conserved, it is uniquely susceptible to evolutionary change. Here we studied three ORF1 proteins: a modern human one (111p), its resuscitated primate ancestor (555p) and a mosaic modern protein (151p) wherein 9 of the 30 coiled coil substitutions retain their ancestral state. While 111p and 555p equally supported retrotransposition, 151p was inactive. Nonetheless, they were fully active in bulk assays of nucleic acid interactions including chaperone activity. However, single molecule assays showed that 151p trimers form stably bound oligomers on ssDNA at <1/10th the rate of the active proteins, revealing that oligomerization rate is a novel critical parameter of ORF1p activity in retrotransposition conserved for at least the last 25 Myr of primate evolution.

Indexed as

Protein MultimerizationDNA, Single-StrandedHumansKineticsLong Interspersed Nucleotide ElementsMolecular ChaperonesOligonucleotidesProtein BindingProteinsDNA, Single-StrandedMolecular ChaperonesOligonucleotidesORF1 protein, humanProteins

Identifiers

PMID26673717
PMCPMC4705668

What OpenQuestion holds

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Registered trials

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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.