Evidence map›Paper›PMID 12208963›Full record

ArticleJournal of virology2002

Flock house virus RNA polymerase is a transmembrane protein with amino-terminal sequences sufficient for mitochondrial localization and membrane insertion.

David J Miller, Paul Ahlquist

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 papers.

0numbers the graph read from it
0cells of the map it votes in
82citing papers in PubMed
6.1field-weighted citation impact, top 4% 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

82 citing papers in PubMed, 125 citations in OpenAlex.

  1. Deciphering theVaccines · 2026
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  6. Nodavirus RNA replication crown architecture reveals proto-crown precursor and viral protein A conformational switching.Proceedings of the National Academy of Sciences of the United States of America · 2023
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  14. Contribution of yeast models to virus research.Applied microbiology and biotechnology · 2021
    Review
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  16. Article
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  19. Review
  20. Article

22 more citing papers are in PubMed but not listed here.

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

2 authors at 1 institution in 2 countries.

David J MillerDepartment of Medicine. Institute for Molecular Virology, University of Wisconsin-Madison, Madison, Wisconsin 53706, USA.
Paul Ahlquist
Institute of Virology of the Slovak Academy of Sciences · SK

Funding

GENE FUNCTIONS AND MOLECULAR GENETICS OF RNA VIRUSESR37GM035072 · NIGMS · UNIVERSITY OF WISCONSIN MADISON · PI AHLQUIST, PAUL G. · 1995 to 2004
$1.9M
GENE FUNCTIONS AND MOLECULAR GENETICS OF RNA VIRUSESR01GM035072 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI AHLQUIST, PAUL G. · 1985 to 2009
$1.6M
HOST-PATHOGEN INTERACTION IN VIRAL REPLICATIONK08AI001770 · NIAID · UNIVERSITY OF WISCONSIN MADISON · PI MILLER, DAVID J · 2000 to 2002
$389k
NIAID NIH HHS K08 AI01770-01NIGMS NIH HHS GM35072NIGMS NIH HHS R01 GM035072NIGMS NIH HHS R37 GM035072
6 · The paper itself

Abstract

Localization of RNA replication to intracellular membranes is a universal feature of positive-strand RNA viruses. Replication complexes of flock house virus (FHV), the best-studied alphanodavirus, are located on outer mitochondrial membranes in infected Drosophila melanogaster cells and are associated with the formation of membrane-bound spherules, similar to structures found for many other positive-strand RNA viruses. To further study FHV replication complex formation, we investigated the subcellular localization, membrane association, and membrane topology of protein A, the FHV RNA-dependent RNA polymerase, in the yeast Saccharomyces cerevisiae, a host able to support full FHV RNA replication and virion formation. Confocal immunofluorescence revealed that protein A localized to mitochondria in yeast, as in Drosophila cells, and that this mitochondrial localization was independent of viral RNA synthesis. Nycodenz gradient flotation and dissociation assays showed that protein A behaved as an integral membrane protein, a finding consistent with a predicted N-proximal transmembrane domain. Protease digestion and selective permeabilization after differential epitope tagging demonstrated that protein A was inserted into the outer mitochondrial membrane with the N terminus in the inner membrane space or matrix and that the C terminus was exposed to the cytoplasm. Flotation and immunofluorescence studies with deletion mutants indicated that the N-proximal region of protein A was important for both membrane association and mitochondrial localization. Gain-of-function studies with green fluorescent protein fusions demonstrated that the N-terminal 46 amino acids of protein A were sufficient for mitochondrial localization and membrane insertion. We conclude that protein A targets and anchors FHV RNA replication complexes to outer mitochondrial membranes, in part through an N-proximal mitochondrial localization signal and transmembrane domain.

Indexed as

Amino Acid SequenceAnimalsDNA-Directed RNA PolymerasesDrosophila melanogasterMembrane ProteinsMitochondriaMolecular Sequence DataNodaviridaeRabbitsRNA, ViralSaccharomyces cerevisiaeViral ProteinsDNA-Directed RNA PolymerasesMembrane ProteinsRNA, ViralViral Proteins

Identifiers

PMID12208963
PMCPMC136485
OpenAlexW2102610618

What OpenQuestion holds

Textmetadata
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.