Algarté M, Kwon H, Génin P, Hiscott J
Terry Fox Molecular Oncology Group, Lady Davis Institute for Medical Research, and Departments of Microbiology & Immunology, Medicine, and Oncology, McGill University, Montreal, Canada H3T 1E2.
Mol Cell Biol. 1999 Sep;19(9):6140-53. doi: 10.1128/MCB.19.9.6140.
In unstimulated cells, NF-kappaB transcription factors are retained in the cytoplasm by inhibitory IkappaB proteins. Upon stimulation by multiple inducers including cytokines or viruses, IkappaBalpha is rapidly phosphorylated and degraded, resulting in the release of NF-kappaB and the subsequent increase in NF-kappaB-regulated gene expression. IkappaBalpha gene expression is also regulated by an NF-kappaB autoregulatory mechanism, via NF-kappaB binding sites in the IkappaBalpha promoter. In previous studies, tetracycline-inducible expression of transdominant repressors of IkappaBalpha (TD-IkappaBalpha) progressively decreased endogenous IkappaBalpha protein levels. In the present study, we demonstrate that expression of TD-IkappaBalpha blocked phorbol myristate acetate-phytohemagglutinin or tumor necrosis factor alpha-induced IkappaBalpha gene transcription and abolished NF-kappaB DNA binding activity, due to the continued cytoplasmic sequestration of RelA(p65) by TD-IkappaBalpha. In vivo genomic footprinting revealed stimulus-responsive protein-DNA binding not only to the -63 to -53 kappaB1 site but also to the adjacent -44 to -36 Sp1 site of the IkappaBalpha promoter. In vivo protection of both sites was inhibited by tetracycline-inducible TD-IkappaBalpha expression. Prolonged NF-kappaB binding and a temporal switch in the composition of NF-kappaB complexes bound to the -63 to -53 kappaB1 site of the IkappaBalpha promoter were also observed; with time after induction, decreased levels of transcriptionally active p50-p65 and increased p50-c-Rel heterodimers were detected at the kappaB1 site. Mutation of either the kappaB1 site or the Sp1 site abolished transcription factor binding to the respective sites and the inducibility of the IkappaBalpha promoter in transient transfection studies. These observations provide the first in vivo characterization of a promoter proximal transcriptional switch involving NF-kappaB and Sp1 that is essential for autoregulation of the IkappaBalpha promoter.
在未受刺激的细胞中,核因子-κB(NF-κB)转录因子被抑制性IκB蛋白保留在细胞质中。在受到包括细胞因子或病毒在内的多种诱导剂刺激后,IκBα会迅速磷酸化并降解,导致NF-κB释放,随后NF-κB调控的基因表达增加。IκBα基因表达也受NF-κB自身调节机制调控,通过IκBα启动子中的NF-κB结合位点实现。在先前的研究中,四环素诱导的IκBα显性负性阻遏物(TD-IκBα)的表达逐渐降低内源性IκBα蛋白水平。在本研究中,我们证明TD-IκBα的表达阻断了佛波酯-植物血凝素或肿瘤坏死因子α诱导的IκBα基因转录,并消除了NF-κB的DNA结合活性,这是由于TD-IκBα持续将RelA(p65)隔离在细胞质中所致。体内基因组足迹分析显示,刺激反应性蛋白-DNA结合不仅发生在IκBα启动子的-63至-53 κB1位点,还发生在相邻的-44至-36 Sp1位点。四环素诱导的TD-IκBα表达抑制了这两个位点的体内保护作用。还观察到IκBα启动子-63至-53 κB1位点的NF-κB结合时间延长以及与之结合的NF-κB复合物组成的时间性转换;诱导后随着时间推移,在κB1位点检测到转录活性p50-p65水平降低,p50-c-Rel异二聚体增加。在瞬时转染研究中,κB1位点或Sp1位点的突变消除了转录因子与各自位点的结合以及IκBα启动子的诱导性。这些观察结果首次在体内对涉及NF-κB和Sp1的启动子近端转录开关进行了表征,该开关对于IκBα启动子的自身调节至关重要。