Tomilin A, Reményi A, Lins K, Bak H, Leidel S, Vriend G, Wilmanns M, Schöler H R
Center for Animal Transgenesis and Germ Cells Research New Bolton Center School of Veterinary Medicine Department of Animal Biology University of Pennsylvania 19348, Kennett Square, PA, USA.
Cell. 2000 Dec 8;103(6):853-64. doi: 10.1016/s0092-8674(00)00189-6.
POU domain proteins contain a bipartite DNA binding domain divided by a flexible linker that enables them to adopt various monomer configurations on DNA. The versatility of POU protein operation is additionally conferred at the dimerization level. The POU dimer formed on the PORE (ATTTGAAATGCAAAT) can recruit the transcriptional coactivator OBF-1, whereas POU dimers formed on the consensus MORE (ATGCATATGCAT) or on MOREs from immunoglobulin heavy chain promoters (AT[G/A][C/A]ATATGCAA) fail to interact. An interaction with OBF-1 is precluded since the same Oct-1 residues that form the MORE dimerization interface are also used for OBF-1/Oct-1 interactions on the PORE. Our findings provide a paradigm of how specific POU dimer assemblies can differentially recruit a coregulatory activity with distinct transcriptional readouts.
POU结构域蛋白包含一个二分DNA结合结构域，该结构域被一个柔性接头分隔开，这使得它们能够在DNA上采用各种单体构型。POU蛋白操作的多功能性还在二聚化水平上得到体现。在PORE（ATTTGAAATGCAAAT）上形成的POU二聚体可以招募转录共激活因子OBF-1，而在共有MORE（ATGCATATGCAT）或免疫球蛋白重链启动子的MOREs（AT[G/A][C/A]ATATGCAA）上形成的POU二聚体则无法相互作用。与OBF-1的相互作用被排除，因为形成MORE二聚化界面的相同Oct-1残基也用于PORE上的OBF-1/Oct-1相互作用。我们的研究结果提供了一个范例，说明特定的POU二聚体组装如何能够以不同的转录读数差异地招募共调节活性。
