First Author | De Haro L | Year | 2002 |
Journal | Nucleic Acids Res | Volume | 30 |
Issue | 13 | Pages | 2972-9 |
PubMed ID | 12087183 | Mgi Jnum | J:210936 |
Mgi Id | MGI:5572895 | Doi | 10.1093/nar/gkf390 |
Citation | De Haro L, et al. (2002) Functional analysis of the transcription factor ER71 and its activation of the matrix metalloproteinase-1 promoter. Nucleic Acids Res 30(13):2972-9 |
abstractText | The ETS transcription factor family is characterized by a conserved ETS DNA-binding domain and its members have been implicated in a plethora of biological processes, including development, cell transformation and metastasis. ER71 is a testis-specific ETS protein that is not homologous to any other protein outside its ETS domain, suggesting that it fulfills a unique physiological role. Here, we report that ER71 is a constitutively nuclear protein whose intracellular localization is dependent on a portion of the ETS domain, namely ER71 amino acids 276-315. Furthermore, the DNA binding activity is intramolecularly regulated, as the N-terminus of ER71 has a negative effect on DNA binding while the C-terminus dramatically enhances this activity. We also demonstrate that ER71 possesses an extremely potent N-terminal transactivation domain comprised of amino acids 1-157. Finally, we show that ER71 is capable of directly activating both an E74 site-driven and the matrix metalloproteinase-1 promoter. Altogether, these data represent the first functional characterization of ER71, which may perform important functions in the developing and adult testis as well as in testicular germ cell tumorigenesis. |