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The Replisome

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An Oligonucleotide-based Tandem RNA Isolation Procedure to Recover Eukaryotic mRNA-Protein Complexes

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Structure of the PCNA unloader Elg1-RFC.

Fengwei Zheng¹, Nina Y Yao², Roxana E Georgescu²

¹Department of Structural Biology, Van Andel Institute, Grand Rapids, MI, USA.

Science Advances

|March 1, 2024

Summary

The Elg1-RFC complex specifically unloads proliferating cell nuclear antigen (PCNA) from DNA. Structural insights reveal unique features, like external loops and an "Elg1 plug," ensuring its dedicated role in PCNA removal.

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Area of Science:

Molecular Biology
Structural Biology
Biochemistry

Background:

DNA replication requires proliferating cell nuclear antigen (PCNA) clamp loading by replication factor C (RFC).
PCNA forms a stable ring around DNA and requires a dedicated complex, Elg1-RFC, for its removal.
Understanding PCNA unloading is crucial for DNA replication fidelity.

Purpose of the Study:

To elucidate the structural basis of Elg1-RFC's dedicated PCNA unloading activity.
To reveal the molecular mechanisms distinguishing PCNA unloading from loading.

Main Methods:

Cryo-electron microscopy (cryo-EM) to determine the structure of Elg1-RFC with PCNA.
Biochemical assays to assess PCNA unloading activity.

Main Results:

The cryo-EM structures revealed unique Elg1-RFC features, including external loops and an "Elg1 plug" domain.
These structural elements were shown to block DNA binding and fill the central chamber, ensuring exclusive PCNA unloading.
Elg1-RFC demonstrated PCNA unloading capability even with non-hydrolyzable AMP-PNP, and both RFC and Elg1-RFC removed PCNA from closed circular DNA.

Conclusions:

Elg1-RFC possesses distinct structural adaptations for dedicated PCNA unloading.
PCNA unloading by Elg1-RFC operates via a mechanism separate from PCNA loading by RFC.
These findings provide critical insights into the regulation of DNA replication and genome stability.