INTERACTIONS OF THE OCT-1 POU SUBDOMAINS WITH SPECIFIC DNA-SEQUENCES AND WITH THE HSV ALPHA-TRANS-ACTIVATOR PROTEIN

被引：207

作者：

KRISTIE, TM ^{[1
]}

SHARP, PA ^{[1
]}

机构：

[1] MIT, DEPT BIOL, CAMBRIDGE, MA 02139 USA

来源：

GENES & DEVELOPMENT | 1990年 / 4卷 / 12B期

关键词：

HERPES SIMPLEX VIRUS; OCTAMER-BINDING PROTEINS; PROTEIN PROTEIN INTERACTIONS; HOMEO BOX; POU DOMAIN; POU-SPECIFIC BOX; PROTEIN-AFFINITY CHROMATOGRAPHY; COOPERATIVE DNA BINDING;

D O I：

10.1101/gad.4.12b.2383

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Trans-activation by the herpes simplex virus (HSV) protein, alpha-TIF(VP16), is dependent on an inducible enhancer sequence that contains a homolog of the octamer element. An ordered series of multiprotein complexes can be assembled on this enhancer, requiring the interactions of Oct-1, alpha-TIF, and two additional cellular factors (C1 and C2). Oct-1 binds to the octamer homolog, whereas alpha-TIF, also a sequence-specific DNA-binding protein, recognizes sequences within the HSV enhancer core. The partially purified C1 factor interacts directly with alpha-TIF in the absence of DNA and is required to form a stabile Oct-1/alpha-TIF/C1 factor complex. The POU domain of Oct-1 is a bipartite sequence recognition structure, as both the POU-specific box and the POU homeo box contribute directly to the recognition of the octamer element. Surprisingly, the POU homeo box alone is sufficient to direct the cooperative binding of alpha-TIF and to assemble the Oct-1/alpha-TIF/C1 factor complex.

引用

页码：2383 / 2396

页数：14

共 79 条

[1] DISTINCT FACTORS WITH SP1 AND NF-A SPECIFICITIES BIND TO ADJACENT FUNCTIONAL ELEMENTS OF THE HUMAN U2 SNRNA GENE ENHANCER [J].