Unknown

Dataset Information

0

Predicting nuclear G-quadruplex RNA-binding proteins with roles in transcription and phase separation.


ABSTRACT: RNA-binding proteins are central for many biological processes and their characterization has demonstrated a broad range of functions as well as a wide spectrum of target structures. RNA G-quadruplexes are important regulatory elements occurring in both coding and non-coding transcripts, yet our knowledge of their structure-based interactions is at present limited. Here, using theoretical predictions and experimental approaches, we show that many chromatin-binding proteins bind to RNA G-quadruplexes, and we classify them based on their RNA G-quadruplex-binding potential. Combining experimental identification of nuclear RNA G-quadruplex-binding proteins with computational approaches, we build a prediction tool that assigns probability score for a nuclear protein to bind RNA G-quadruplexes. We show that predicted G-quadruplex RNA-binding proteins exhibit a high degree of protein disorder and hydrophilicity and suggest involvement in both transcription and phase-separation into membrane-less organelles. Finally, we present the G4-Folded/UNfolded Nuclear Interaction Explorer System (G4-FUNNIES) for estimating RNA G4-binding propensities at http://service.tartaglialab.com/new_submission/G4FUNNIES .

SUBMITTER: Luige J 

PROVIDER: S-EPMC10959947 | biostudies-literature | 2024 Mar

REPOSITORIES: biostudies-literature

altmetric image

Publications

Predicting nuclear G-quadruplex RNA-binding proteins with roles in transcription and phase separation.

Luige Johanna J   Armaos Alexandros A   Tartaglia Gian Gaetano GG   Ørom Ulf Andersson Vang UAV  

Nature communications 20240322 1


RNA-binding proteins are central for many biological processes and their characterization has demonstrated a broad range of functions as well as a wide spectrum of target structures. RNA G-quadruplexes are important regulatory elements occurring in both coding and non-coding transcripts, yet our knowledge of their structure-based interactions is at present limited. Here, using theoretical predictions and experimental approaches, we show that many chromatin-binding proteins bind to RNA G-quadrupl  ...[more]

Similar Datasets

| S-EPMC7145655 | biostudies-literature
| S-EPMC4227175 | biostudies-literature
2020-05-12 | GSE150399 | GEO
| S-EPMC4041461 | biostudies-literature
| S-EPMC6460439 | biostudies-literature
| S-EPMC9825518 | biostudies-literature
| S-EPMC8197425 | biostudies-literature
| S-EPMC6063760 | biostudies-literature
| S-EPMC6031325 | biostudies-literature
| S-EPMC11312991 | biostudies-literature