title: Functional analysis of the transcription factor ER71 and its activation of the matrix metalloproteinase-1 promoter.
abstract: 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.
authors.affiliation: Department of Biochemistry and Molecular Biology, Guggenheim Building 1501A, Mayo Clinic and Mayo Graduate School, 200 First Street SW, Rochester, MN 55905, USA.
authors.forename: Luciano
authors.initials: L
authors.lastname: De Haro
authors.forename: Ralf
authors.initials: R
authors.lastname: Janknecht
mesh_terms: D000818:Animals; D001665:Binding Sites / Q000235:genetics; D001667:Binding, Competitive; D002460:Cell Line; D002466:Cell Nucleolus / Q000378:metabolism; D002467:Cell Nucleus / Q000378:metabolism; D024202:Electrophoretic Mobility Shift Assay; D005786:Gene Expression Regulation; D049452:Green Fluorescent Proteins; D006801:Humans; D008156:Luciferases / Q000235:genetics / Q000378:metabolism; D008164:Luminescent Proteins / Q000235:genetics / Q000378:metabolism; D020781:Matrix Metalloproteinase 1 / Q000235:genetics*; D008856:Microscopy, Fluorescence; D009841:Oligonucleotides / Q000235:genetics / Q000378:metabolism; D011401:Promoter Regions, Genetic / Q000235:genetics*; D011485:Protein Binding; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D014157:Transcription Factors / Q000235:genetics / Q000502:physiology*; D014158:Transcription, Genetic; D014162:Transfection; D014407:Tumor Cells, Cultured
chemical_list: D008164:Luminescent Proteins; D009841:Oligonucleotides; D011993:Recombinant Fusion Proteins; D014157:Transcription Factors; D049452:Green Fluorescent Proteins; D008156:Luciferases; D020781:Matrix Metalloproteinase 1