Evidence map›Paper›PMID 8649422›Full record

ArticleMolecular and cellular biology1996

Sex-specific and non-sex-specific oligomerization domains in both of the doublesex transcription factors from Drosophila melanogaster.

W An, S Cho, H Ishii, P C Wensink

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Article in Molecular and cellular biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
1.1field-weighted citation impact, top 22% of its field
1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

Who cites it

35 citing papers in PubMed, 80 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

4 authors at 1 institution in 1 country.

W AnDepartment of Biochemistry, Brandeis University, Waltham, Massachusetts 02254-9110, USA.
S Cho
H Ishii
P C Wensink
Brandeis University · US

Funding

SEX-SPECIFIC REGULATION OF TRANSCRIPTION IN DROSOPHILAR01GM046237 · NIGMS · BRANDEIS UNIVERSITY · PI WENSINK, PIETER C · 1991 to 1998
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NIGMS NIH HHS GM46237
6 · The paper itself

Abstract

The doublesex gene of Drosophila melanogaster encodes the alternatively spliced, sex-specific transcription factors DSXM and DSXF. These factors regulate male- and female-specific transcription of many genes. For example, female-specific transcription of the yolk protein 1 gene is regulated by DSXM repression in males and DSXF activation in females. In this study we used in vitro interaction assays and the in vivo yeast two-hybrid method to identify and examine oligomerization domains of the DSX proteins. A 66-amino-acid segment common to both proteins (amino acids 39 to 104) contains a sequence-specific DNA binding domain and an oligomerization domain (OD1). The OD1 domain oligomerizes up to at least a pentamer, but only dimers bound to a palindromic regulatory site in the yolk protein 1 gene are detected. Both subunits of the OD1 dimer are in contact with DNA. Another segment of each protein (amino acids 350 to 412 for DSXF and 350 to 427 for DSXM) contains a second oligomerization domain (OD2F and OD2M, respectively). The OD2 domains have both sex-specific and non-sex-specific sequences which are necessary for oligomerization. On the basis of sequence analysis, we predict that OD2 oligomerizes through coiled-coil interactions. We speculate that the common function of OD1 and OD2 is to oligomerize the full-length proteins, whereas their specialized functions are to form a dimeric DNA binding unit and a sex-specific transcriptional activation or repression unit.

Indexed as

Drosophila ProteinsAmino Acid SequenceAnimalsBase SequenceBinding SitesDNADNA-Binding ProteinsDNA PrimersDrosophila melanogasterFemaleInsect HormonesMaleMolecular Sequence DataProtein ConformationSex CharacteristicsTranscription FactorsDNADNA-Binding ProteinsDNA PrimersDrosophila ProteinsDSX protein, DrosophilaInsect HormonesTranscription Factors

Identifiers

PMID8649422
PMCPMC231305
OpenAlexW2100115704

What OpenQuestion holds

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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.