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Related Experiment Video

Updated: Jan 22, 2026

Genome Editing with CompoZr Custom Zinc Finger Nucleases ZFNs

Genome Editing with CompoZr Custom Zinc Finger Nucleases ZFNs

Published on: June 14, 2012

PRDM9 forms a trimer by interactions within the zinc finger array.

Theresa Schwarz¹, Yasmin Striedner¹, Andreas Horner¹

¹Institute of Biophysics, Johannes Kepler University, Linz, Austria.

Life Science Alliance

|July 17, 2019

Summary

This summary is machine-generated.

The protein PRDM9, crucial for DNA repair during meiosis, forms a stable trimer. This multimerization, driven by its zinc finger array, ensures accurate DNA binding for genetic recombination.

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Area of Science:

Molecular Biology
Genetics
Biochemistry

Background:

PRDM9 is a key protein regulating meiotic recombination.
Its multimeric state and the factors driving multimerization were previously unknown.

Purpose of the Study:

To determine the stoichiometry of PRDM9 multimers.
To investigate the role of the zinc finger (ZnF) array in PRDM9 multimerization and DNA binding.

Main Methods:

In vitro binding studies
Electrophoretic mobility shift assays (EMSA)
Mass spectrometry
Fluorescence correlation spectroscopy (FCS)

Main Results:

PRDM9 forms a stable trimer in solution, independent of DNA binding.
The variable zinc finger (ZnF) array of PRDM9 is sufficient for trimer formation.
At least five ZnFs are required for a functional trimer.
Only one ZnF array within the trimer binds DNA, while others mediate protein-protein interactions.

Conclusions:

PRDM9 exists as a trimer, a state adopted by the soluble protein.
The ZnF array is critical for both PRDM9 multimerization and DNA targeting.
PRDM9's trimeric structure facilitates specific DNA binding for meiotic recombination.