The High Mobility Group Protein 1 Enhances Binding of the Estrogen Receptor DNA Binding Domain to the Estrogen Response Element
نویسندگان
چکیده
منابع مشابه
The high mobility group protein 1 enhances binding of the estrogen receptor DNA binding domain to the estrogen response element.
We have examined the ability of the high-mobility group protein 1 (HMG1) to alter binding of the estrogen receptor DNA-binding domain (DBD) to the estrogen response element (ERE). HMG1 dramatically enhanced binding of purified, bacterially expressed DBD to the consensus vitellogenin A2 ERE in a dose-dependent manner. The ability of HMG1 to stabilize the DBD-ERE complex resulted in part from a d...
متن کاملMouse Estrogen Receptor b Forms Estrogen Response Element- Binding Heterodimers with Estrogen Receptor a
The recent discovery that an additional estrogen receptor subtype is present in various rat tissues has advanced our understanding of the mechanisms underlying estrogen signaling. Here we report on the cloning of the cDNA encoding the mouse homolog of estrogen receptor-b (ERb) and the functional characterization of mouse ERb protein. ERb is shown to have overlapping DNA-binding specificity with...
متن کاملEstrogen activates the high-density lipoprotein receptor gene via binding to estrogen response elements and interaction with sterol regulatory element binding protein-1A.
The effects of E2 on the high-density lipoprotein receptor (HDL-R) scavenger receptor class B type I (SR-BI) gene were examined. Four putative estrogen response element half-site motifs (ERE(1/2)) (-2176, -1726, -1622, and -1211, designated ERE(1/2)-1, 2, 3, and 4, respectively) were identified in the HDL-R SR-BI promoter. Transfection studies and mutation analysis demonstrated that E2 signific...
متن کاملRNA inhibits estrogen receptor binding to DNA.
Cytosol from MTW9 rat mammary tumor contains a high molecular weight inhibitor of estrogen receptor binding to DNA. RNase treatment of crude preparations destroys inhibitory activity, whereas DNase or trypsin treatment are without affect, suggesting that some RNA molecule might be involved; in addition, RNA extracted from tumor cytosol was an effective inhibitor of estrogen receptor binding to ...
متن کاملHigh mobility group B proteins facilitate strong estrogen receptor binding to classical and half-site estrogen response elements and relax binding selectivity.
The estrogen receptor alpha (ER) is a ligand-dependent transcription factor that regulates the expression of estrogen-responsive genes. A key step in the activation process is the initial binding of the ER dimer to the estrogen response element (ERE). We examined the effect of the coactivator proteins, HMGB1 and HMGB2, in enhancing ER binding affinity to single and tandem EREs. Using EMSAs, bot...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Molecular Endocrinology
سال: 1998
ISSN: 0888-8809,1944-9917
DOI: 10.1210/mend.12.5.0111