Identification of a novel protein from glial cells based on its ability to interact with NF-kappaB subunits

Nuclear factor kappaB (NF-kappaB) represents a family of inducible DNA-binding transcription factors whose activity is critical for expression of the HIV-1 genome in a broad range of cells. In addition to its interaction with the kappaB DNA sequence, the association of NF-kappaB subunits with other...

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Bibliographic Details
Published in:Journal of cellular biochemistry 2003-12, Vol.90 (5), p.884-891
Main Authors: Sweet, Thersa, Khalili, Kamel, Sawaya, Bassel E, Amini, Shohreh
Format: Article
Language:English
Subjects:
Astrocytes - metabolism
Cell Nucleolus - metabolism
Cells, Cultured - metabolism
Cells, Cultured - virology
Chromosomes, Human, Pair 10 - genetics
Gene Library
Glutathione Transferase - metabolism
HIV-1 - genetics
Humans
Neuroglia - metabolism
NF-kappa B - physiology
NF-kappa B p50 Subunit
Nuclear Proteins - genetics
Nuclear Proteins - metabolism
Promoter Regions, Genetic
Protein Binding
Saccharomyces cerevisiae
Transcription Factor RelA
Two-Hybrid System Techniques
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Summary:Nuclear factor kappaB (NF-kappaB) represents a family of inducible DNA-binding transcription factors whose activity is critical for expression of the HIV-1 genome in a broad range of cells. In addition to its interaction with the kappaB DNA sequence, the association of NF-kappaB subunits with other cellular proteins plays an important role in stimulation of HIV-1 gene transcription in astrocytic cells. Here, we utilized a yeast two-hybrid system to screen a cDNA library from a human astrocytic cell line and were able to isolate a partial cDNA belonging to a gene with an open reading frame of 1,871 amino acid residues which binds to both the p50 and p65 subunits of NF-kappaB. This gene, named NF-kappaB-binding protein (NFBP) is located on chromosome 10q24.2-25.1 and hybridized to a single transcript of nearly 6 kb in size. It is localized to the nucleus, specifically the nucleolus of cells. Extensive computer analysis was performed with the sequence of the full length NFBP and significant homology was found between NFBP, and yeast and mouse proteins. A discussion of the potential roles of NFBP in normal and viral infected cells is included.
ISSN:0730-2312
1097-4644