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Related Concept Videos

Protein Complex Assembly02:41

Protein Complex Assembly

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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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...
Protein Complex Assembly02:41

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Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach
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Protein-dependent transition states for ribonucleoprotein assembly.

A E Webb1, M A Rose, E Westhof

  • 1Department of Chemistry, University of North Carolina, Chapel Hill, NC 27599-3290, USA.

Journal of Molecular Biology
|June 12, 2001
PubMed
Summary

Saccharomyces cerevisiae CBP2 and Neurospora crassa CYT-18 protein cofactors facilitate group I intron RNA folding and splicing. CYT-18 protein binds rapidly but assembles slowly, unlike CBP2, revealing distinct cofactor mechanisms.

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Area of Science:

  • Molecular Biology
  • RNA Biology
  • Biochemistry

Background:

  • Group I introns are self-splicing RNAs found in various organisms.
  • Protein cofactors like CBP2 and CYT-18 are essential for the proper folding and splicing of mitochondrial group I introns.
  • Understanding cofactor-RNA interactions is crucial for elucidating RNA catalytic mechanisms.

Purpose of the Study:

  • To compare the distinct mechanisms by which Saccharomyces cerevisiae CBP2 and Neurospora crassa CYT-18 protein cofactors assemble with the bI5 group I intron RNA.
  • To investigate the kinetic and thermodynamic properties of these assembly processes.
  • To determine how these differences in assembly impact RNA folding and catalytic activity.

Main Methods:

  • Time-resolved footprinting to visualize RNA folding during protein assembly.
  • Partitioning experiments to determine kinetic parameters (k(off)/k(on)).
  • Kinetic and thermodynamic analyses (activation enthalpy) of protein-RNA complex formation.

Main Results:

  • Both CBP2 and CYT-18 facilitate bI5 RNA splicing at similar rates, suggesting similar active site structures.
  • CBP2 assembly is limited by a slow RNA folding step with low activation enthalpy.
  • CYT-18 exhibits rapid, stable binding but slow assembly, characterized by a large activation enthalpy and a distinct kinetic signature, with potential for CYT-18 to catalyze RNA folding at elevated temperatures.

Conclusions:

  • CBP2 and CYT-18 proteins assemble with the bI5 group I intron RNA via distinct mechanisms.
  • CYT-18's assembly pathway involves rapid protein binding followed by a rate-limiting RNA conformational rearrangement.
  • The differential assembly mechanisms highlight the diverse strategies employed by protein cofactors to facilitate RNA function.