Cotranslational biogenesis of NF-κB p50 by the 26S proteasome
Cotranslational biogenesis of NF-κB p50 by the 26S proteasome
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DOI：
10.1016/s0092-8674(00)81409-9
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发表时间：
1998-03-20
期刊：
影响因子：
64.5
通讯作者：
Greene, WC
中科院分区：
文献类型：
--
作者：
Lin, L;DeMartino, GN;Greene, WC
NFKB1基因编码两种功能不同的蛋白质，分别称为p50和p105。P50对应于p105的N端，与p65(RelA)形成典型的核因子-kappaB转录因子复合体。相比之下，p105作为一种REL特异性抑制物(I Kappa B)发挥作用，并被认为是p50的前体。我们的研究表明，p50是由涉及26S蛋白酶体的独特的共翻译加工事件产生的，而p50 C末端附近的序列的共翻译折叠放弃了蛋白酶体加工酸导致p105的产生。这些结果表明p105不是p50的前体，并揭示了一种新的基因调控机制，确保了p50和p105蛋白的平衡生产和独立功能。
The NFKB1 gene encodes two functionally distinct proteins termed p50 and p105. p50 corresponds to the N terminus of p105 and with p65 (RelA) forms the prototypical NF-kappa B transcription factor complex. In contrast, p105 functions as a Rel-specific inhibitor (I kappa B) and has been proposed to be the precursor of p50. Our studies now demonstrate that p50 is generated by a unique cotranslational processing event involving the 26S proteasome, whereas cotranslational folding of sequences near the C terminus of p50 abrogates proteasome processing acid leads to p105 production. These results indicate that p105 is not the precursor of p50 and reveal a novel mechanism of gene regulation that ensures the balanced production and independent function of the p50 and p105 proteins.