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Related Experiment Video

Updated: Jun 6, 2025

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Structural proteomics defines a sequential priming mechanism for the progesterone receptor.

Patrick Griffin1, Matthew Mann2, Min Wang2

  • 1UF Scripps Biomedical Research Institute.

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|November 28, 2024
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Summary

This study reveals how progesterone receptor (PR) isoforms interact with co-regulatory proteins (CoRs) using structural mass spectrometry. Findings challenge current models by showing persistent CoR interactions even with antagonist-bound PR.

Keywords:
Progesterone receptorcrosslinkinghydrogen-deuterium exchangemass spectrometrynuclear receptorsprotein-protein interactionstranscriptional co-regulatory proteins

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DNA Sequence Recognition by DNA Primase Using High-Throughput Primase Profiling
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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • The progesterone receptor (PR) is a nuclear receptor with two isoforms, PR-A and PR-B.
  • Disruption of PR signaling is linked to breast cancer via interactions with co-regulatory proteins (CoRs).
  • Molecular details of isoform-specific PR-CoR interactions are not well understood.

Purpose of the Study:

  • To investigate the sequential binding mechanism of PR isoforms and CoRs (SRC3 and p300) on target DNA.
  • To elucidate the structural basis of PR-CoR interactions during transcriptional complex assembly.
  • To understand the role of PR conformation in CoR binding.

Main Methods:

  • Structural mass spectrometry was employed to study purified full-length PR and intact CoRs.
  • Analysis focused on complexes formed on target DNA.
  • Peptide-level analysis provided insights into protein organization and interactions.

Main Results:

  • Selective NR-box binding by PR to CoRs was observed.
  • Unique interaction surfaces between PR and CoRs were identified during complex assembly.
  • Antagonist-bound PR exhibited persistent CoR interactions, contrary to classical models.

Conclusions:

  • The study provides a peptide-level perspective on the PR transcriptional complex organization.
  • It offers a structural basis for sequential CoR binding to PR.
  • Findings challenge established models of nuclear receptor activation and repression by revealing persistent CoR interactions in inactive conformations.