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Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
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Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

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BRMS151-98 and BRMS151-84 are crystal oligomeric coiled coils with different oligomerization states, which behave as

Mercedes Spínola-Amilibia1, José Rivera, Miguel Ortiz-Lombardía

  • 1Instituto de Biomedicina de Valencia (IBV-CSIC), C/Jaime Roig 11, 46010 Valencia, Spain.

Journal of Molecular Biology
|March 19, 2013
PubMed

Insights

Breast cancer metastasis suppressor 1 (BRMS1) protein localization is key to inhibiting metastasis. Its N-terminal coiled coil structure may facilitate nuclear export, impacting metastasis suppression.

Area of Science:

  • Molecular Biology
  • Cancer Research
  • Structural Biology

Background:

  • Breast cancer metastasis suppressor 1 (BRMS1) inhibits tumor metastasis without impacting primary tumor growth.
  • BRMS1's cellular localization is critical for its metastasis-suppressing function.
  • BRMS1 undergoes nucleo-cytoplasmic shuttling, mediated by a nuclear export signal in its N-terminal coiled coil.

Purpose of the Study:

  • To investigate the structural and biophysical characteristics of the BRMS1 N-terminal coiled coil.
  • To understand how this region contributes to BRMS1's biological function in metastasis inhibition.
  • To explore the role of specific residues (85-98) in the oligomerization state and function of BRMS1.

Main Methods:

  • Structural and biophysical analyses of the BRMS1 N-terminal coiled coil region.
  • Investigation of protein fragments and their behavior in solution.
  • Characterization of conformational dynamics and oligomerization states.

Main Results:

  • The N-terminal coiled coil of BRMS1 can oligomerize, potentially hindering nuclear export signal accessibility.
  • Residues 85-98 appear crucial for determining the oligomerization state of the N-terminal coiled coil.
  • BRMS1 fragments are largely disordered in solution but exhibit residual structure.
  • A conformational dynamic equilibrium (folded ↔ unfolded oligomeric species) was observed in the N-terminal coiled coil in solution.

Conclusions:

  • The N-terminal coiled coil's structure and dynamics influence BRMS1's oligomerization and nuclear export.
  • The observed conformational equilibrium may facilitate BRMS1's transport to the cytoplasm, contributing to metastasis suppression.
  • Understanding these structural features provides insights into the mechanism of BRMS1-mediated metastasis inhibition.

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