Abstract
THE transcription factor NF-κB is a heterodimer consisting of two proteins encoded by different members of the rel gene family (p50 and p65)1–7. The p50 subunit is unusual among DNA-binding proteins in that its functional form is encoded in an open reading frame of relative molecular mass 105,000 (p105; ref. 4). The N-terminal region of this open reading frame encodes p50, whereas the remaining C terminus contains ankyrin repeats. Although p50 binds to DNA, full-length p105 translated in vitro does not4,5. The mechanism by which p50 is generated in vivo, and the fate of the C-terminal region of p105 have not been established. Here we show that functional p50 is produced by ATP-dependent pro-teolysis of p105. Moreover, we find that the C-terminal half of p105 is not required for processing in vivo, and is rapidly degraded on processing. We propose that the C-terminal region of p105 is involved in the cytoplasmic assembly of the complex between the p50/p65 heterodimer and the inhibitor IkB.
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Fan, CM., Maniatis, T. Generation of p50 subunit of NF-kB by processing of p105 through an ATP-dependent pathway. Nature 354, 395–398 (1991). https://doi.org/10.1038/354395a0
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DOI: https://doi.org/10.1038/354395a0
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