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First published in Nucleic Acids Research, v52 (2024) published by Oxford University Press. DOI: https://doi.org/10.1093/nar/gkae834

Document Type

Article

Publication Version

Published Version

Keywords

Genome integrity, repair and replication

Journal/Book/Conference Title

Nucleic Acids Research

Volume

52

Issue

20

First Page

12422

Last Page

12437

Abstract

Human replication protein A (RPA) is a heterotrimeric ssDNA binding protein responsible for many aspects of cellular DNA metabolism. Dynamic interactions of the four RPA DNA binding domains (DBDs) with DNA control replacement of RPA by downstream proteins in various cellular metabolic pathways. RPA plays several important functions at telomeres where it binds to and melts telomeric G-quadruplexes, non-canonical DNA structures formed at the G-rich telomeric ssDNA overhangs. Here, we combine single-molecule total internal reflection fluorescence microscopy (smTIRFM) and mass photometry (MP) with biophysical and biochemical analyses to demonstrate that heterogeneous nuclear ribonucleoprotein A1 (hnRNPA1) specifically remodels RPA bound to telomeric ssDNA by dampening the RPA configurational dynamics and forming a ternary complex. Uniquely, among hnRNPA1 target RNAs, telomeric repeat-containing RNA (TERRA) is selectively capable of releasing hnRNPA1 from the RPA-telomeric DNA complex. We speculate that this telomere specific RPA-DNA-hnRNPA1 complex is an important structure in telomere protection.

Department

Department of Physics

Original Publication Date

11-11-2024

Object Description

1 PDF File

DOI of published version

10.1093/nar/gkae834

Repository

UNI ScholarWorks, Rod Library, University of Northern Iowa

Copyright

©2024 The Author(s) This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial License.

Creative Commons License

Creative Commons Attribution-NonCommercial 4.0 International License
This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License

Language

en

File Format

application/pdf

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