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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.
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The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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Dynamic assembly of a large multidomain ribozyme visualized by cryo-electron microscopy.

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This study reveals how complex RNA molecules assemble sequentially to avoid non-functional states. Key structural motifs guide this process, creating a molecular movie of RNA folding.

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Area of Science:

  • Structural Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Many functional RNAs depend on precise 3D structures.
  • RNAs can form non-functional misfolded states ('kinetic traps') during folding.
  • Sequential assembly over scaffolds is an alternative folding pathway.

Purpose of the Study:

  • To elucidate the principles of RNA sequential assembly.
  • To understand how RNAs avoid misfolded states.
  • To visualize the assembly of a self-splicing ribozyme.

Main Methods:

  • Single-particle electron cryomicroscopy (cryo-EM)
  • Small-angle X-ray scattering (SAXS)
  • EM-driven molecular dynamics (MD) simulations
  • Structure-based mutagenesis
  • Enzymatic assays

Main Results:

  • Visualized the sequential multidomain assembly of a self-splicing ribozyme.
  • Identified a dynamic interplay of helical subdomains in the 5'-scaffold controlling domain docking.
  • Discovered conserved secondary structure motifs orchestrating conformational changes for catalytic pocket formation.

Conclusions:

  • RNA sequential assembly avoids non-functional 'kinetic traps'.
  • Specific structural motifs are crucial for guiding RNA folding pathways.
  • Provides a near-atomic resolution molecular movie of large multidomain RNA assembly.