Cloning of the p50 DNA binding subunit of NF-κB: Homology to rel and dorsal

Ghosh, Sankar; Gifford, Ann; Riviere, Lise R.; Tempst, Paul; Nolan, Garry P.; Baltimore, David

doi:10.1016/0092-8674(90)90276-k

Cited by 843 publications

(487 citation statements)

References 38 publications

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“…The identified members of this family are NF-KB1 (p50), p5OB,p52), RelA (p65), RelB and cRel (Nabel and Verma, 1993). NF-KB1 and 2 are both synthesized as precursor proteins (p105-NF-KB1 and p00-NF-KB2, respectively) and need to be proteolytically processed for maturation (Bours et al, 1990Gosh et al, 1990; Kieran et al, 1990;Meyer et al, 1991;Neri et al, 1991). No such processing events are required for the other Rel proteins.…”

Section: Introductionmentioning

confidence: 99%

Two distinct mechanisms contribute to the constitutive activation of RelB in lymphoid cells.

Lernbecher¹,

Kistler²,

Wirth³

1994

The EMBO Journal

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Section: Introductionmentioning

confidence: 99%

Two distinct mechanisms contribute to the constitutive activation of RelB in lymphoid cells.

Lernbecher¹,

Kistler²,

Wirth³

1994

The EMBO Journal

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“…In many unstimulated cells, NF-KB is found localized to the cytoplasm as a latent heterodimeric complex bound to its subunit-specific inhibitor IKB (also called MAI)-3) (11). dsRNA treatment of 70Z/3 pre-B-lymphocytes leads to the activation and translocation of transcription factor NF-KB to the nucleus, where it binds its cognate DNA element, positive regulatory domain II (PRDII) (11)(12)(13). NF-KB in conjunction with transcription factors highmobility group 1, activating transcription factor 2, IFN regulatory factor 1 (IRF-1), and c-jun product activates the 8 promoter (14).…”

mentioning

confidence: 99%

Double-stranded RNA-dependent protein kinase activates transcription factor NF-kappa B by phosphorylating I kappa B.

Kumar

Haque

Lacoste

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

519

409

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The induction of interferon (IN) genes by viruses or double-stranded RNA (dsRNA) requires the assembly of a complex set of trnscription factors on responsive DNA elements of ION gene promoters. One of the factors necessary for regulating IFN-P gene transcription is nuclear factor NF-KB, the activation of which is triggered by dsRNA. It has previously been suggested that the dsRNA-activated p68 protein kinase (PKR) may act as an Inducer-receptor, transducing the signal from dsRNA to NF-ucB through phosphorylation of the inhibitor IKB. We present direct evidence that PKR can phosphorylate IKB-a (MAD-3) and activate NF-KB DNA binding activity in vitro. We further show that dsRNA induces an unusual phosphorylated form of IKB-a. The expression of a transdominant mutant PKR is able to perturb the dsRNAmediated signaling pathway in vivo, suggesting a role for this kinase in IFN-P gene induction.

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“…The ReIA(p65) and RelB subunits are most highly homologous to c-Rel (49,58,59,61) and contain transactivation domains in their carboxy termini (12,27,31,49,55,60,61,63). Two related cDNAs encoding the larger precursor proteins of the 50-kDa DNAbinding subunits of NF-KB, NF-KB1(p105) (10,22,34,44) and NF-KB2(plOO) (9,47,62), have been isolated. Both gene products require proteolytic processing to generate the -50-kDa amino terminus DNA-binding forms, NF-KB1(pSO) and NF-KB2(p52) (8,19,43).…”

mentioning

confidence: 99%

An interaction between the DNA-binding domains of RelA(p65) and Sp1 mediates human immunodeficiency virus gene activation.

Perkins¹,

Agranoff²,

Pascal³

et al. 1994

Mol. Cell. Biol.

225

157

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Induction of human immunodeficiency virus type 1 (HIV-1) gene expression in stimulated T cells has been attributed to the activation of the transcription factor NF-KB. The twice-repeated KB sites within the HIV-1 long terminal repeat are in close proximity to three binding sites for Spl. We have previously shown that a cooperative interaction of NF-KB with Spl is required for the efficient stimulation of HIV-1 transcription. In this report, we define the domains of each protein responsible for this effect. Although the transactivation domains seemed likely to mediate this interaction, we find, surprisingly, that this interaction occurs through the putative DNA-binding domains of both proteins. Spl specifically interacted with the amino-terminal region of ReIA(p65). Similarly, RelA bound directly to the zinc finger region of Spl. This interaction was specific and resulted in cooperative DNA binding to the icB and Spl sites in the HIV-1 long terminal repeat. Furthermore, the amino-terminal region of RelA did not associate with several other transcription factors, including MyoD, E12, or Koxl5, another zinc finger protein. These findings suggest that the juxtaposition of DNA-binding sites promotes a specific protein interaction between the DNA-binding regions of these transcription factors. This interaction is required for HIV transcriptional activation and may provide a mechanism to allow for selective activation of KB-regulated genes.

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Cloning of the p50 DNA binding subunit of NF-κB: Homology to rel and dorsal

Cited by 843 publications

References 38 publications

Two distinct mechanisms contribute to the constitutive activation of RelB in lymphoid cells.

Two distinct mechanisms contribute to the constitutive activation of RelB in lymphoid cells.

Double-stranded RNA-dependent protein kinase activates transcription factor NF-kappa B by phosphorylating I kappa B.

An interaction between the DNA-binding domains of RelA(p65) and Sp1 mediates human immunodeficiency virus gene activation.

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