Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Analysis of estrogen receptor interaction with tertiary-structured estrogen responsive elements

D A Lannigan1, J J Tomashek, J D Obourn

  • 1Department of Zoology, University of Vermont, Burlington 05405.

Biochemical Pharmacology
|May 5, 1993
PubMed
Summary

The estrogen receptor preferentially binds to DNA sequences with tertiary structures, known as estrogen-responsive elements (EREs). ERE flanking sequences also influence receptor binding affinity and interaction types.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Multisubstrate isotope labeling and metagenomic analysis of active soil bacterial communities.

mBio·2014
Same author

The serine/threonine protein kinase, p90 ribosomal S6 kinase, is an important regulator of prostate cancer cell proliferation.

Cancer research·2005
Same author

Stoichiometry of energy coupling by proton-translocating ATPases: a history of variability.

Journal of bioenergetics and biomembranes·2004
Same author

Characterization of reconstituted Fo from wild-type Escherichia coli and identification of two other fluxes co-purifying with Fo.

Cell biochemistry and biophysics·2002
Same author

Rsk2 allosterically activates estrogen receptor alpha by docking to the hormone-binding domain.

The EMBO journal·2001
Same author

A functional His-tagged c subunit of the Escherichia coli F-type ATPase/Synthase.

Archives of biochemistry and biophysics·2001

Area of Science:

  • Molecular Biology
  • Genetics
  • Endocrinology

Background:

  • Estrogen receptor (ER) binding to estrogen-responsive elements (EREs) is critical for estrogen-mediated gene regulation.
  • Previous studies indicated preferential ER binding to a specific imperfect ERE with tertiary structure.

Purpose of the Study:

  • To investigate ER interaction with both perfect and imperfect EREs possessing tertiary structures.
  • To determine the role of ERE sequence deviations and flanking sequences in ER binding affinity.

Main Methods:

  • Utilized perfect and imperfect EREs from the chicken vitellogenin II gene.
  • Synthesized a 42 bp oligonucleotide mimicking a perfect ERE lower strand with flanking sequences.

Main Results:

Related Experiment Videos

  • Estrogen receptor preferentially binds to EREs, both perfect and imperfect, that exhibit tertiary structure.
  • Deviations from the ERE consensus sequence reduce ER binding to tertiary-structured EREs.
  • ERE flanking sequences significantly contribute to ER binding affinity and interaction specificity with tertiary-structured EREs.

Conclusions:

  • Tertiary structure is a key determinant for estrogen receptor binding to EREs.
  • ERE sequence and flanking regions modulate the affinity and nature of ER-ERE interactions, impacting gene regulation.