Synergism with the coactivator OBF-1 (OCA-B, BOB-1) is mediated by a specific POU dimer configuration

被引：112

作者：

Tomilin, A

Reményi, A

Lins, K

Bak, H

Leidel, S

Vriend, G

Wilmanns, M

Schöler, HR ^{[1
]}

机构：

[1] Univ Penn, New Bolton Ctr, Sch Vet Med,Dept Anim Biol, Ctr Anim Transgenesis & Germ Cells Res, Kennett Square, PA 19348 USA

[2] European Mol Biol Lab, Gene Express Programme, D-69117 Heidelberg, Germany

[3] European Mol Biol Lab, Biocomp Programme, D-69117 Heidelberg, Germany

[4] DESY, EMBL, Hamburg Outstn, D-2263 Hamburg, Germany

来源：

CELL | 2000年 / 103卷 / 06期

关键词：

D O I：

10.1016/S0092-8674(00)00189-6

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 (ATGCATATG CAT) 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.

引用

页码：853 / 864

页数：12

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