THE OCT-1 POU DOMAIN MEDIATES INTERACTIONS BETWEEN OCT-1 AND OTHER POU PROTEINS

被引：82

作者：

VERRIJZER, CP ^{[1
]}

VANOOSTERHOUT, JAWM ^{[1
]}

VANDERVLIET, PC ^{[1
]}

机构：

[1] UNIV UTRECHT, PHYSIOL CHEM LAB, VONDELLAAN 24A, 3521 GG UTRECHT, NETHERLANDS

来源：

MOLECULAR AND CELLULAR BIOLOGY | 1992年 / 12卷 / 02期

关键词：

D O I：

10.1128/MCB.12.2.542

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：

The POU domain is the conserved DNA binding domain of a family of gene regulatory proteins. It consists of a POU-specific domain and a POU homeodomain, connected by a variable linker region. Oct-1 is a ubiquitously expressed POU domain transcription factor. It binds to the canonical octamer sequence (ATGCAAAT) as a monomer. Here we show by chemical cross-linking and protein affinity chromatography that the Oct-1 POU domain monomers can interact in solution. This association requires both the POU homeodomain and the POU-specific domain. The interaction is transient in solution and can be stabilized by binding to the heptamer-octamer sequence in the immunoglobulin heavy-chain promoter. This correlates with cooperative DNA binding to this site. POU proteins from different subclasses, including Oct-1, Oct-2A, Oct-6, and a chimeric Oct-1 protein containing the Pit-1 POU domain, can bind cooperatively to a double binding site and form a heteromeric complex.

引用

页码：542 / 551

页数：10

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