HMG boxes of DSP1 protein interact with the Rel homology domain of transcription factors
Autor: | D. Locker, M. Leng, C. Mosrin-Huaman, M. J. Giraud-Panis, Martine Decoville |
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Přispěvatelé: | Centre de biophysique moléculaire (CBM), Université d'Orléans (UO)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC) |
Jazyk: | angličtina |
Rok vydání: | 2000 |
Předmět: |
animal structures
HMG-box [SDV]Life Sciences [q-bio] Molecular Sequence Data Biology Article Rel homology domain 03 medical and health sciences 0302 clinical medicine Genetics Animals Drosophila Proteins Amino Acid Sequence Binding site Cloning Molecular Transcription factor Psychological repression 030304 developmental biology DNA Primers 0303 health sciences Binding Sites Base Sequence fungi High Mobility Group Proteins Nuclear Proteins Phosphoproteins Molecular biology Proto-Oncogene Proteins c-rel 3. Good health Rats Drosophila melanogaster 030220 oncology & carcinogenesis Drosophila Protein Morphogen Transcription Factors |
Zdroj: | Nucleic Acids Research Nucleic Acids Research, Oxford University Press, 2000, 28 (2), pp.454-462. ⟨10.1093/nar/28.2.454⟩ Europe PubMed Central |
ISSN: | 0305-1048 1362-4962 |
DOI: | 10.1093/nar/28.2.454⟩ |
Popis: | International audience; Formation of the dorsoventral axis in Drosophila melanogaster is mediated through control of the expression of several genes by the morphogen Dorsal. In the ventral part of the embryo Dorsal activates twist and represses zen amongst others. Recently, several proteins have been shown to assist Dorsal in the repression of zen, one of which is DSP1, a HMG box protein that was isolated as a putative co-repressor of Dorsal. In this report we used a DSP1 null mutant to ascertain in vivo the involvement of DSP1 in Dorsal-mediated repression of zen but not in the activation of twist. We show that Dorsal has the ability to interact with DSP1 in vitro as well as with rat HMG1. Using truncated versions of the proteins we located the domains of interaction as being the HMG boxes for DSP1 and HMG1 and the Rel domain for Dorsal. Finally, studies of the zen DNA binding properties of Dorsal and another related Rel protein (Gambif1 from Anopheles gambiae) revealed that their DNA binding affinities were increased in the presence of DSP1 and HMG1. |
Databáze: | OpenAIRE |
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