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The Yeast Prefoldin Bud27.

Verónica Martínez-Fernández1, Ana Isabel Garrido-Godino1, Abel Cuevas-Bermudez1

  • 1Departamento de Biología Experimental, Facultad de Ciencias Experimentales, Universidad de Jaén, Jaén, Spain.

Advances in Experimental Medicine and Biology
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PubMed
Summary
This summary is machine-generated.

Bud27 and its human counterpart URI are molecular chaperones that bind RNA polymerases. Their distinct interactions suggest novel roles beyond co-chaperoning, highlighting functional differences across species.

Keywords:
Bud27Chromatin remodelerPrefoldin-likeRNA polymerasesRNA polymerases assemblyRibosome biogenesisRpb5Saccharomyces cerevisiaeTOR pathwayTranscription

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Bud27 and its human orthologue URI are ATP-independent molecular chaperones belonging to the prefoldin family.
  • They bind the Rpb5 subunit, associating with all nuclear eukaryotic RNA polymerases.
  • Bud27/URI are thought to scaffold other prefoldin family members, but are not part of the canonical PFD/GimC complex.

Purpose of the Study:

  • To investigate the composition and function of Bud27/URI-containing complexes.
  • To compare the interactions of Bud27 in yeast with its human orthologue URI.
  • To clarify the role of Bud27/URI in relation to the PFD/GimC and R2TP/PFDL complexes.

Main Methods:

  • Comparative analysis of protein-protein interactions.
  • Investigation of molecular chaperone complex composition.
  • Functional studies of Bud27 and URI in yeast and human systems.

Main Results:

  • Bud27 interacts specifically with Pfd6, and previously reported interactions with Pfd2 were not confirmed.
  • Significant differences exist in prefoldin-like complex composition between yeast and other organisms.
  • The R2TP/PFDL complex, differing across species, has not been identified in yeast.

Conclusions:

  • Bud27/URI interactions differ from canonical prefoldin complexes, suggesting unique functions.
  • Species-specific variations in prefoldin-like and R2TP/PFDL complexes impact Bud27/URI function.
  • Bud27/URI may have critical cellular roles independent of, and more significant than, previously proposed co-prefoldin functions.