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Related Concept Videos

Ribozymes02:47

Ribozymes

The term ribozyme is used for RNA that can act as an enzyme. Ribozymes are mainly found in selected viruses, bacteria, plant organelles, and lower eukaryotes. Ribozymes were first discovered in 1982 when Tom Cech’s laboratory observed Group I introns acting as enzymes. This was shortly followed by the discovery of another ribozyme, Ribonulcease P, by Sid Altman’s laboratory. Both Cech and Altman received the Nobel Prize in chemistry in 1989 for their work on ribozymes.
Ribozymes can be...
Ribozymes02:47

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The term ribozyme is used for RNA that can act as an enzyme. Ribozymes are mainly found in selected viruses, bacteria, plant organelles, and lower eukaryotes. Ribozymes were first discovered in 1982 when Tom Cech’s laboratory observed Group I introns acting as enzymes. This was shortly followed by the discovery of another ribozyme, Ribonulcease P, by Sid Altman’s laboratory. Both Cech and Altman received the Nobel Prize in chemistry in 1989 for their work on ribozymes.
Ribozymes can be...
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Protein Folding

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Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
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Protein-facilitated ribozyme folding and catalysis.

Nora Zingler1, Amanda Solem, Anna Marie Pyle

  • 1Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520, USA. nora.zingler@yale.edu

Nucleic Acids Symposium Series (2004)
|September 9, 2008
PubMed
Summary

Large RNAs need proteins for proper folding in vivo. We investigated whether the Mss116 protein stabilizes or disrupts intermediates of the S. cerevisiae group II intron ai5 gamma to promote its active structure.

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Area of Science:

  • Molecular Biology
  • RNA Folding
  • Protein-RNA Interactions

Background:

  • Large RNAs, such as introns, require protein assistance for correct three-dimensional folding in vivo.
  • The DEAD-box protein Mss116 is known to facilitate the folding of the S. cerevisiae group II intron ai5 gamma into its catalytically active conformation.

Purpose of the Study:

  • To experimentally distinguish between two proposed mechanisms by which Mss116 promotes intron folding: stabilizing on-pathway intermediates versus disrupting misfolded structures.
  • To clarify the precise role of Mss116 in the in vivo folding pathway of the ai5 gamma intron.

Main Methods:

  • Review and analysis of existing experimental data.
  • Interpretation of evidence related to Mss116's function in RNA folding.

Main Results:

  • The presented evidence allows for a distinction between Mss116 acting as a stabilizer of productive folding intermediates or as a disruptor of non-productive, misfolded states.
  • Discussion of the implications of each potential mechanism for understanding protein-mediated RNA folding.

Conclusions:

  • The precise mechanism by which Mss116 facilitates the folding of the ai5 gamma intron remains a subject for further investigation.
  • Understanding Mss116's role is crucial for deciphering the general principles of protein-assisted RNA folding in biological systems.