Rnf4, a RING protein expressed in the developing nervous and reproductive systems, interacts with Gscl, a gene within the DiGeorge critical region.
A yeast 2-hybrid screen was performed to identify possible transcriptional modulators interactive with goosecoid-like (gscl), a transcription factor with suppressive activity, expressed during early brain and gonad development. The screen resulted in the identification of a RING protein known as rnf4 or snrf. Gscl/rnf4 interactions were confirmed by affinity chromatography ... and by immunoprecipitation. Northern analysis confirmed earlier reports of ubiquitous rnf4 expression in adult tissues. Immunohistochemical analysis of mouse embryos revealed expression primarily in the developing nervous system, with strong expression in the dorsal root ganglia and developing gonads. In contrast to previous reports, both cytoplasmic and nuclear expression of rnf4 was documented. The results reported here confirm and extend earlier reports of rnf4 expression. They suggest for the first time, that in addition to acting as a modulator of transcriptional activity, rnf4 may function, as do other RING proteins, to promote the formation of intracytoplasmic complexes involved in shuttling information between the cytoplasm and the nucleus.
Mesh Terms:
Animals, Binding Sites, Blotting, Northern, COS Cells, Cell Nucleus, Cytoplasm, DNA, Complementary, DNA-Binding Proteins, DiGeorge Syndrome, Ganglia, Spinal, Gene Expression Regulation, Developmental, Gonads, Goosecoid Protein, Homeodomain Proteins, In Situ Hybridization, Male, Mice, Molecular Sequence Data, Nuclear Proteins, Prostate, RNA, Messenger, Repressor Proteins, Sequence Homology, Amino Acid, Structure-Activity Relationship, Testis, Transcription Factors, Transfection, Two-Hybrid System Techniques
Animals, Binding Sites, Blotting, Northern, COS Cells, Cell Nucleus, Cytoplasm, DNA, Complementary, DNA-Binding Proteins, DiGeorge Syndrome, Ganglia, Spinal, Gene Expression Regulation, Developmental, Gonads, Goosecoid Protein, Homeodomain Proteins, In Situ Hybridization, Male, Mice, Molecular Sequence Data, Nuclear Proteins, Prostate, RNA, Messenger, Repressor Proteins, Sequence Homology, Amino Acid, Structure-Activity Relationship, Testis, Transcription Factors, Transfection, Two-Hybrid System Techniques
Dev. Dyn.
Date: May. 01, 2000
PubMed ID: 10822263
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