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Related Experiment Video

Updated: Jul 6, 2026

Eukaryotic Polyribosome Profile Analysis

Published on: June 16, 2010

A chaperone for ribosome maturation.

A I Lalev¹, R N Nazar

¹Department of Molecular Biology and Genetics, University of Guelph, Guelph, Ontario N1G 2W1, Canada.

The Journal of Biological Chemistry

|March 30, 2001

Summary

A novel ribosome assembly chaperone (RAC) complex binds all transcribed spacers in precursor ribosomal RNA. This protein complex is crucial for eukaryotic ribosome maturation and acts as a quality control mechanism.

Area of Science:

Molecular Biology
Biochemistry
Cell Biology

Background:

Eukaryotic ribosome synthesis involves processing precursor ribosomal RNA (pre-rRNA) into mature ribosomal RNA (rRNA).
pre-rRNA processing is interdependent and acts as a quality control mechanism for ribosome assembly.
The internal transcribed spacers (ITS) of pre-rRNA are critical for this processing.

Purpose of the Study:

To identify proteins involved in pre-rRNA processing.
To investigate the role of internal transcribed spacers in ribosome assembly.
To characterize the structure and function of the ribosome assembly chaperone (RAC) complex.

Main Methods:

Affinity chromatography using Schizosaccharomyces pombe internal transcribed spacer 1 (ITS1) and ITS2 as ligands.

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Isolation and characterization of protein complexes.

Competition binding assays to determine spacer binding specificity.

Main Results:

A large spliceosome-like protein complex, the ribosome assembly chaperone (RAC), composed of over 20 polypeptides, was isolated.
The RAC complex contains independent binding sites for all four transcribed spacers in the pre-rRNA.
Disruption of these binding sites severely affects rRNA processing.

Conclusions:

The RAC complex is a key chaperone for ribosome maturation in eukaryotes.
The RAC complex organizes critical structure in pre-rRNA, acting as a "rack" for ribosome assembly.
This complex plays a vital role in ensuring the fidelity of ribosome biogenesis.