Evidence map›Paper›PMID 9847304›Full record

ArticleJournal of virology1999

Targeting of the visna virus tat protein to AP-1 sites: interactions with the bZIP domains of fos and jun in vitro and in vivo.

B A Morse, L M Carruth, J E Clements

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 1999. 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
5.2field-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

9 citing papers in PubMed, 23 citations in OpenAlex.

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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 at 1 institution in 1 country.

B A MorseDivision of Comparative Medicine, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
L M Carruth
J E Clements
Johns Hopkins University · US

Funding

REGULATING GENE EXPRESSION OF NEUROTROPIC LENTIVIRUSESR01NS023039 · NINDS · JOHNS HOPKINS UNIVERSITY · PI CLEMENTS, JANICE ELLEN · 1986 to 2004
$1.6M
MOLECULAR PATHOGENESIS OF AIDS RELATED CNS DISEASET32NS007392 · NINDS · JOHNS HOPKINS UNIVERSITY · PI CLEMENTS, JANICE ELLEN · 1995 to 2005
$895k
NINDS NIH HHS NS07392NINDS NIH HHS NS23039NINDS NIH HHS R01 NS023039NINDS NIH HHS T32 NS007392
6 · The paper itself

Abstract

The visna virus Tat protein is required for efficient viral transcription from the visna virus long terminal repeat (LTR). AP-1 sites within the visna virus LTR, which can be bound by the cellular transcription factors Fos and Jun, are also necessary for Tat-mediated transcriptional activation. A potential mechanism by which the visna virus Tat protein could target the viral promoter is by protein-protein interactions with Fos and/or Jun bound to AP-1 sites in the visna virus LTR. Once targeted to the visna virus promoter, the Tat protein could then interact with basal transcription factors to activate transcription. To examine protein-protein interactions with cellular proteins at the visna virus promoter, we used an in vitro protein affinity chromatography assay and electrophoretic mobility shift assay, in addition to an in vivo two-hybrid assay, to show that the visna virus Tat protein specifically interacts with the cellular transcription factors Fos and Jun and the basal transcription factor TBP (TATA binding protein). The Tat domain responsible for interactions with Fos and Jun was localized to an alpha-helical domain within amino acids 34 to 69 of the protein. The TBP binding domain was localized to amino acids 1 to 38 of Tat, a region previously described by our laboratory as the visna virus Tat activation domain. The bZIP domains of Fos and Jun were found to be important for the interactions with Tat. Mutations within the basic domains of Fos and Jun abrogated binding to Tat in the in vitro assays. The visna virus Tat protein was also able to interact with covalently cross-linked Fos and Jun dimers. Thus, the visna virus Tat protein appears to target AP-1 sites in the viral promoter in a mechanism similar to the interaction of human T-cell leukemia virus type 1 Tax with the cellular transcription factor CREB, by binding the basic domains of an intact bZIP dimer. The association between Tat, Fos, and Jun would position Tat proximal to the viral TATA box, where the visna virus Tat activation domain could contact TBP to activate viral transcription.

Indexed as

Terminal Repeat SequencesAnimalsBasic-Leucine Zipper Transcription FactorsBinding SitesDNA-Binding ProteinsG-Box Binding FactorsGene Products, tatHumansProto-Oncogene Proteins c-fosProto-Oncogene Proteins c-junSheepTATA-Box Binding ProteinTranscription FactorsVisna-maedi virusBasic-Leucine Zipper Transcription FactorsDNA-Binding ProteinsG-Box Binding FactorsGene Products, tatProto-Oncogene Proteins c-fosProto-Oncogene Proteins c-junTATA-Box Binding ProteinTranscription Factors

Identifiers

PMID9847304
PMCPMC103805
OpenAlexW1539162151

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.