Potter D A, Larson C J, Eckes P, Schmid R M, Nabel G J, Verdine G L, Sharp P A
Center for Cancer Research, Massachusetts Institute of Technology, Cambridge 02139.
J Biol Chem. 1993 Sep 5;268(25):18882-90.
H2TF1 is a ubiquitous major histocompatibility complex (MHC) class I-specific transcription factor, which binds to the palindromic kappa B enhancer site upstream of MHC class I genes. Here we report that H2TF1 consists of a polypeptide with relative molecular mass 110,000, that corresponds to the predicted 100-kDa product (NF-kappa B2 p100) encoded by the candidate proto-oncogene nfkb2 (lyt-10). H2TF1 was purified by a novel affinity chromatography method and identified as the NF-kappa B2 p100 polypeptide by peptide sequencing as well as by reactivity with a specific antiserum. Purified H2TF1 binds the MHC kappa B site with high affinity (KD = 3 x 10(-11) M), in contrast with previous reports that NF-kappa B2 p100 did not bind DNA.
H2TF1是一种普遍存在的主要组织相容性复合体(MHC)I类特异性转录因子,它与MHC I类基因上游的回文κB增强子位点结合。在此我们报告,H2TF1由一种相对分子质量为110,000的多肽组成,该多肽对应于候选原癌基因nfkb2(lyt - 10)编码的预测100 kDa产物(NF-κB2 p100)。通过一种新型亲和层析方法纯化了H2TF1,并通过肽序列分析以及与特异性抗血清的反应性将其鉴定为NF-κB2 p100多肽。纯化的H2TF1以高亲和力(KD = 3×10⁻¹¹ M)结合MHC κB位点,这与之前关于NF-κB2 p100不结合DNA的报道相反。