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Related Experiment Videos

Multiple functions of an evolutionarily conserved RNA binding domain.

J Vilardell1, S J Yu, J R Warner

  • 1Department of Cell Biology, Albert Einstein College of Medicine, Bronx, New York 10461, USA.

Molecular Cell
|July 6, 2000
PubMed
Summary

Archaeal and yeast ribosomal protein L30 bind the same RNA structure, inhibiting gene expression. This conserved interaction suggests L30

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Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • Ribosomal protein L30 (L30) in Saccharomyces cerevisiae regulates its own gene expression via RNA binding.
  • This autoregulation involves binding to a specific RNA structure, inhibiting splicing and translation.

Purpose of the Study:

  • To investigate the evolutionary conservation of L30's RNA binding specificity.
  • To determine if archaeal L30 orthologs can regulate yeast gene expression.
  • To identify the conserved RNA target and its functional significance in ribosome biogenesis.

Main Methods:

  • In vitro RNA binding assays.
  • In vivo gene expression and growth assays in yeast.
  • Bioinformatic analysis of conserved RNA structures and protein orthologs.

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Main Results:

  • The archaeal L30 from Sulfolobus acidocaldarius specifically binds the same RNA structure as yeast L30.
  • Expression of archaeal L30 in yeast inhibits endogenous L30 production and severely impairs cell growth.
  • The conserved RNA target site is located in a region crucial for inter-subunit bridges in the ribosome.

Conclusions:

  • The RNA binding specificity of ribosomal protein L30 is highly conserved across archaea and eukaryotes.
  • This conservation highlights a fundamental regulatory mechanism likely established over a billion years ago.
  • L30 plays a critical role in ribosome assembly, potentially by orienting key structural elements between ribosomal subunits.