Binding properties of the human homeodomain protein OTX2 to a DNA target sequence

FEBS Letters

Briata, Paola²  Ilengo, Cristina²  Bobola, Nicoletta¹  Corte, Giorgio² 

[1] Department of Clinical and Experimental Oncology, University of Genova, Genova, Italy;Immunobiology Laboratory, IST-National Institute for Cancer Research, Advanced Biotechnology Center, Largo Rosanna Benzi, 10, 16132 Genova, Italy

关键词: OTX2;    Homeodomain;    DNA binding;    Dimer;    Development;   

DOI  :  10.1016/S0014-5793(99)00113-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

OTX2, a homeodomain protein essential in mouse for the development of structures anterior to rhombomere 3, binds with high affinity to a DNA element (called OTS) present in the human tenascin-C promoter. Here we investigate the binding properties of the full length recombinant human OTX2 and of several deletion mutants to the OTS element. We demonstrate that, upon binding of the protein to its DNA target site, a second molecule of OTX2 is recruited to the complex and that a nearby second binding site is not necessary for this interaction. OTX2 sequences located within a region carboxyl-terminal to the homeodomain are necessary in addition to the homeodomain for binding to DNA. Furthermore, OTX2 dimerization requires the same protein domains necessary for DNA binding.

【 授权许可】

Unknown