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PXL: a Nucleic Acid-Binding Module of Promyelocytic Leukemia Protein.

Daniel Fairchild¹, Irina V Semenova¹, Dane Geddes-Buehre¹

¹Department of Molecular Biology and Biophysics, School of Medicine, University of Connecticut, 263 Farmington Avenue, Farmington, CT, 06030, United States.

Biorxiv : the Preprint Server for Biology

|February 27, 2026

Summary

The promyelocytic leukemia protein isoform 1 (PML-1) has a novel nucleic acid-binding module, PXL, that binds G-rich RNA and DNA. This discovery reveals a new molecular function for PML in gene regulation and nuclear organization.

Keywords:

DNA binding G-quadruplex PML isoforms PML-1 Promyelocytic leukemia (PML)RNA binding RNAseq X-ray crystallography protein structure pseudo-nuclease transcription

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Area of Science:

Molecular biology
Cell biology
Structural biology

Background:

The promyelocytic leukemia protein (PML) is a key stress-response factor.
PML forms nuclear bodies involved in tumor suppression and antiviral defense.
The functions of the abundant PML-1 isoform are not fully understood at a molecular level.

Purpose of the Study:

To elucidate the molecular mechanisms underlying the functions of the PML-1 protein.
To identify and characterize novel nucleic acid-binding capabilities of PML-1.

Main Methods:

X-ray crystallography to determine the 3D structure of the PXL module.
Biochemical assays and mutational analyses to assess nucleic acid binding.
RNA sequencing (RNA-seq) to analyze transcriptome modulation.

Main Results:

A unique nucleic acid-binding module, PXL, was identified within PML-1.
The PXL module selectively binds single-stranded G-rich RNA and DNA motifs.
PML-1 binding to these motifs was shown to modulate the cellular transcriptome.

Conclusions:

PML-1 possesses an unexpected molecular function mediated by the PXL module.
This finding provides a structural and functional basis for PML's roles in nuclear organization and gene regulation.
The PXL module's interaction with nucleic acids offers new insights into PML's involvement in cellular stress responses.