Lenardo M J, Kuang A, Gifford A, Baltimore D
Whitehead Institute for Biomedical Research, Cambridge, MA 02142.
Haematol Blood Transfus. 1989;32:411-5. doi: 10.1007/978-3-642-74621-5_71.
To characterize the NF-kappa B binding factor in molecular terms and to facilitate the cloning of its gene, we have purified this protein from bovine spleen tissue. We have found it is a 42,000-dalton protein that exists in solution as a dimer. We were able to use the purified protein to show that the same polypeptide is able to recognize sites important for activation of genes in either B- or T-lymphocytes. Moreover, we were able to define a consensus sequence which allows ascertainment of a wider variety of sequences that are capable of interacting with this protein. The implication of the same protein in gene regulation in two different lineages of lymphoid cells reveals an unexpected unity in the mechanism of gene expression during B- and T-lymphocyte activation. This also suggests that other regulatory events must participate with NF-kappa B activation in determining B- or T-cell-specific expression.
为了从分子层面表征核因子κB结合因子并促进其基因的克隆，我们从牛脾脏组织中纯化了这种蛋白质。我们发现它是一种42,000道尔顿的蛋白质，在溶液中以二聚体形式存在。我们能够利用纯化后的蛋白质证明，同一多肽能够识别对B淋巴细胞或T淋巴细胞中基因激活至关重要的位点。此外，我们能够确定一个共有序列，从而能够确定更多能够与该蛋白质相互作用的序列。同一蛋白质参与两种不同淋巴细胞谱系的基因调控，这揭示了B淋巴细胞和T淋巴细胞激活过程中基因表达机制出人意料的一致性。这也表明，在决定B细胞或T细胞特异性表达方面，其他调控事件必须与核因子κB激活共同发挥作用。
