Human RelB (I-Rel) functions as a kappa B site-dependent transactivating member of the family of Rel-related proteins.
RelB belongs to the family of Rel-related proteins, dimers of which determine NF-kappa B activity. The murine RelB protein has been reported to be a dimerizing partner in kappa B-binding complexes which are capable of transactivation. On the other hand, the I-Rel protein, the presumed human homolog of RelB, was proposed to be an inhibitor whose presence in dimeric complexes interfered with their kappa B binding and therefore interfered also with transactivation. We demonstrate that human RelB (I-Rel) forms with p50 and p52 (p50B) kappa B-binding heterodimeric complexes which potently transactivate kappa B-dependent constructs in transfection studies. It is concluded that human RelB (I-Rel) and murine RelB can both function as transactivators and that no significant species-specific differences exist.
Bours
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Laboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892.
Azarenko
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V
Dejardin
E
E
Siebenlist
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U
D000818:Animals; D001483:Base Sequence; D004247:DNA / Q000378:metabolism; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D016328:NF-kappa B / Q000378:metabolism*; D011518:Proto-Oncogene Proteins; D013045:Species Specificity; D015534:Trans-Activators / Q000502:physiology*; D051841:Transcription Factor RelB; D014157:Transcription Factors / Q000502:physiology*; D014162:Transfection
D016328:NF-kappa B; D011518:Proto-Oncogene Proteins; C497593:RELB protein, human; C497594:Relb protein, mouse; D015534:Trans-Activators; D014157:Transcription Factors; D051841:Transcription Factor RelB; D004247:DNA