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Related Experiment Video

Updated: May 5, 2026

Novel RNA-Binding Proteins Isolation by the RaPID Methodology

Novel RNA-Binding Proteins Isolation by the RaPID Methodology

Published on: September 30, 2016

Rrp5 binding at multiple sites coordinates pre-rRNA processing and assembly.

Simon Lebaron¹, Asa Segerstolpe², Sarah L French³

¹Wellcome Trust Centre for Cell Biology, University of Edinburgh, Michael Swann Building, Kings Buildings, Mayfield Road, Edinburgh EH9 3JR, Scotland.

|November 19, 2013

Summary

This summary is machine-generated.

The ribosome synthesis factor Rrp5 binds pre-ribosomal RNA (pre-rRNA) and coordinates its processing. Its N- and C-terminal domains direct specific cleavage events essential for ribosome biogenesis.

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Novel RNA-Binding Proteins Isolation by the RaPID Methodology

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Published on: September 30, 2016

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A Rapid High-throughput Method for Mapping Ribonucleoproteins RNPs on Human pre-mRNA

A Rapid High-throughput Method for Mapping Ribonucleoproteins RNPs on Human pre-mRNA

Published on: December 2, 2009

Area of Science:

Molecular Biology
Biochemistry
Genetics

Background:

Ribosome biogenesis is a complex, highly regulated process crucial for cell viability.
The ribosome synthesis factor Rrp5 is essential for preribosomal RNA (pre-rRNA) processing.
Understanding Rrp5's function requires detailed mapping of its interactions within the preribosome.

Purpose of the Study:

To identify pre-rRNA binding sites for Rrp5 using in vivo UV crosslinking.
To elucidate the distinct roles of Rrp5's N-terminal domain (NTD) and C-terminal domain (CTD) in pre-rRNA cleavage.
To investigate Rrp5's role in coordinating preribosomal assembly and processing.

Main Methods:

In vivo UV crosslinking to map Rrp5-pre-rRNA interactions.
Intramolecular complementation assays to assess functional domains of Rrp5.
Analysis of Rrp5 interactions with small nucleolar RNAs (snoRNAs) and ribonuclease MRP.
Chromatin spread analysis to evaluate Rrp5's role in preribosome structure.

Main Results:

Numerous pre-rRNA binding sites for Rrp5 were identified.
Rrp5's CTD is crucial for cleavage at sites A0-A2, interacting with flanking sequences and essential snoRNAs (U3, U14, snR30, snR10).
Rrp5's NTD is required for A3 cleavage, interacting with flanking sequences and ribonuclease MRP.
Rrp5 also interacts with structural proteins and nucleoside triphosphatases, and its depletion disrupts cotranscriptional cleavage and preribosome compaction.

Conclusions:

Rrp5 acts as a key coordinator of pre-rRNA processing and ribosome assembly.
Distinct domains of Rrp5 mediate specific interactions with different pre-rRNA regions and processing factors.
Rrp5's function is critical for the structural integrity and efficient processing of preribosomes.