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Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella
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Crystal Structure of the Human Ribosome in Complex with DENR-MCT-1

Ivan B Lomakin1, Elena A Stolboushkina2, Anand T Vaidya1

  • 1Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114, USA.

Cell Reports
|July 21, 2017
PubMed

Insights

The density-regulated protein (DENR)-malignant T cell-amplified sequence 1 (MCT-1) complex binds ribosomes to control cancer-related mRNA translation. Structural analysis reveals its ribosome interaction site, offering insights into translation initiation mechanisms.

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Cancer Research

Background:

  • Density-regulated protein (DENR) and malignant T cell-amplified sequence 1 (MCT-1/MCTS1) oncoprotein regulate cancer-related mRNA translation.
  • DENR and MCT-1 form a heterodimer that binds ribosomes, influencing translation initiation and reinitiation.

Purpose of the Study:

  • To determine the crystal structure of the human small ribosomal subunit in complex with the DENR-MCT-1 dimer.
  • To elucidate the binding site and mechanism of DENR-MCT-1 interaction with the ribosome.

Main Methods:

  • X-ray crystallography
  • Structural analysis of protein-ribosome complex

Main Results:

  • The crystal structure of the human small ribosomal subunit complexed with DENR-MCT-1 was determined.
  • The DENR-MCT-1 dimer binds to the small ribosomal subunit.
  • The DENR C-terminal domain binding site on the ribosome resembles that of translation initiation factor 1 (eIF1).

Conclusions:

  • The study reveals the structural basis of DENR-MCT-1 interaction with the ribosome.
  • Findings provide insights into the mechanism of unconventional translation initiation and reinitiation.
  • This structural information has implications for understanding cancer-related translational control.
Keywords:
density regulated proteinmalignant T cell-amplified sequence 1protein synthesisribosometranslation initiationtranslation reinitiation

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