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Related Experiment Videos

A La protein requirement for efficient pre-tRNA folding.

Ghadiyaram Chakshusmathi1, Sang Do Kim, Douglas A Rubinson

  • 1Departments of Cell Biology and Molecular Biophysics and Biochemistry, Howard Hughes Medical Institute, Yale University School of Medicine, 295 Congress Avenue, New Haven, CT 06536, USA.

The EMBO Journal
|December 6, 2003
PubMed
Summary

The La protein, Lhp1p, is crucial for proper pre-transfer RNA (tRNA) folding, particularly for tRNA(Arg)(CCG). This protein ensures efficient tRNA aminoacylation and cell growth, especially under cold stress.

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Area of Science:

  • Molecular Biology
  • RNA Biology
  • Yeast Genetics

Background:

  • The La protein (Lhp1p in yeast) is known to protect nascent small RNAs.
  • Efficient RNA folding is critical for cellular function and requires precise three-dimensional structures.

Purpose of the Study:

  • To investigate the role of the La protein (Lhp1p) in pre-transfer RNA (tRNA) folding.
  • To elucidate the mechanism by which Lhp1p assists in tRNA maturation and function.

Main Methods:

  • Yeast genetics: utilized cold-sensitive mutants and gene depletion strategies.
  • Biochemical assays: performed chemical and enzymatic footprinting to analyze RNA structure.
  • In vitro refolding experiments: assessed pre-tRNA folding under various conditions.

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Main Results:

  • A mutation in pre-tRNA(Arg)(CCG) led to cold sensitivity and dependence on Lhp1p for growth.
  • The mutation caused misfolding of the pre-tRNA(Arg)(CCG) anticodon stem, which was rescued by suppressor mutations.
  • Lhp1p was shown to stabilize the correct pre-tRNA stem structure, facilitating efficient aminoacylation.

Conclusions:

  • The La protein (Lhp1p) is essential for the efficient folding of specific pre-tRNAs, including tRNA(Arg)(CCG).
  • Pre-tRNAs can misfold in vivo, and protein chaperones like Lhp1p are required to ensure correct folding and function.
  • This study reveals a novel role for the La protein in assisting pre-tRNA folding beyond its known function in 3' end protection.