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Related Experiment Videos

Structural basis for mRNA recognition by elongation factor SelB.

Satoko Yoshizawa1, Linda Rasubala, Toyoyuki Ose

  • 1Laboratoire de RMN, Institut de Chimie des Substances Naturelles, Centre National de la Recherche Scientifique, 1 Avenue de la Terrasse, 91190 Gif-sur-Yvette, France. yoshizawa@icsn.cnrs-gif.fr

Nature Structural & Molecular Biology
|January 25, 2005
PubMed
Summary
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Bacterial selenocysteine incorporation relies on elongation factor SelB, which binds mRNA hairpin structures. Researchers determined the crystal structure of SelB

Area of Science:

  • Molecular biology
  • Structural biology
  • Biochemistry

Background:

  • Selenocysteine is the 21st amino acid, incorporated into proteins in bacteria.
  • Elongation factor SelB facilitates selenocysteine incorporation by binding both tRNA and mRNA.
  • The molecular basis for SelB's specific binding to the selenocysteine insertion sequence (SECIS) RNA hairpin was previously unknown.

Purpose of the Study:

  • To determine the crystal structure of the mRNA-binding domain of SelB in complex with SECIS RNA.
  • To elucidate the molecular basis of SelB's specific RNA recognition.

Main Methods:

  • X-ray crystallography
  • Determination of the crystal structure of the SelB-SECIS RNA complex at 2.3 A resolution.

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Main Results:

  • The crystal structure of the SelB winged-helix (WH) domain in complex with SECIS RNA was determined.
  • This represents the first structure of an RNA-WH domain complex.
  • RNA binding did not induce significant conformational changes in the WH domain.
  • A novel RNA recognition mode was revealed, with a geometry enabling the complex to wrap around the small ribosomal subunit.

Conclusions:

  • The determined structure provides insights into the molecular mechanism of specific mRNA recognition by SelB.
  • This finding reveals a new mode of RNA recognition by a WH domain.
  • The structural data explains how SelB specifically binds SECIS RNA to facilitate selenocysteine incorporation.