Evidence map›Paper›PMID 17005674›Full record

ArticleJournal of virology2006

Catalytic core of alphavirus nonstructural protein nsP4 possesses terminal adenylyltransferase activity.

Shailly Tomar, Richard W Hardy, Janet L Smith, Richard J Kuhn

Abstract read
In one paragraph

Article in Journal of virology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
91citing papers in PubMed, 1 pooled it
5.3field-weighted citation impact, top 5% 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

91 citing papers in PubMed, 1 synthesis or guideline pooled it, 149 citations in OpenAlex.

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31 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

4 authors at 3 institutions in 1 country.

Shailly TomarDepartment of Biological Sciences, Purdue University, 915 W. State Street, West Lafayette, IN 47907-2054, USA.
Richard W Hardy
Janet L Smith
Richard J Kuhn
Purdue University West Lafayette · USIndiana University Bloomington · USUniversity of Michigan–Ann Arbor · US

Funding

Structure-function studies of alpha-and flavivirusesP01AI055672 · NIAID · PURDUE UNIVERSITY WEST LAFAYETTE · PI KUHN, RICHARD J. · 2003 to 2010
$18.4M
NIAID NIH HHS P01 AI 055672NIAID NIH HHS P01 AI055672
6 · The paper itself

Abstract

The RNA-dependent RNA polymerase nsP4 is an integral part of the alphavirus replication complex. To define the role of nsP4 in viral RNA replication and for a structure-function analysis, we expressed Sindbis virus nsP4 in Escherichia coli. The core catalytic domain of nsP4 (Delta97nsP4, a deletion of the N-terminal 97 amino acids), which consists of the predicted polymerase domain containing the GDD amino acid motif required for viral RNA synthesis, was stable against proteolytic degradation during expression. Therefore, the recombinant core domain and selected mutants were expressed and purified to homogeneity. We determined that Delta97nsP4 possesses terminal adenylyltransferase (TATase) activity, as it specifically catalyzed the addition of adenine to the 3' end of an acceptor RNA in the presence of divalent cations. Furthermore, Delta97nsP4 is unable to transfer other nucleotides (UTP, CTP, GTP, and dATP) to the acceptor RNA in the absence or presence of other nucleotides. Delta97nsP4 possessing a GDD-to-GAA mutation completely inactivates the enzymatic activity. However, a GDD-to-SNN mutation did not inactivate the enzyme but reduced its activity to approximately 45% of that of the wild type in the presence of Mg(2+). Investigation of the TATase of the GDD-to-SNN mutant revealed that it had TATase equivalent to that of the wild type in the presence of Mn(2+). Identification of Delta97nsP4 TATase activity suggests a novel function of the alphavirus RNA-dependent RNA polymerase in the maintenance and repair of the poly(A) tail, an element required for replication of the viral genome.

Indexed as

Sindbis VirusAdenineAmino Acid SubstitutionCatalytic DomainCations, DivalentCloning, MolecularCoenzymesDNA Mutational AnalysisEscherichia coliGene ExpressionMutation, MissenseNucleotidyltransferasesRecombinant ProteinsRNASequence DeletionSubstrate SpecificityAdenineCations, DivalentCoenzymesglutamine-synthetase adenylyltransferasensP4 protein, Sindbis virusNucleotidyltransferasesRecombinant ProteinsRNAViral Nonstructural Proteins

Identifiers

PMID17005674
PMCPMC1617302
OpenAlexW2107250397

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.