{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"submitter":["Guzman BB"],"funding":["NHLBI NIH HHS","NIGMS NIH HHS"],"pubmed_abstract":["RNA binding proteins (RBPs) interact with and tightly regulate the fate of messenger RNAs but how RNA targets are recognized remains a challenging question. RBPs often contain multiple domains known to directly bind RNA, such as RNA recognition motifs (RRMs), as well as domains whose RNA binding capacity remains incompletely understood, <i>e.g.,</i> low complexity domains (LCDs). Here, we dissect HNRNPR, an RBP with three RRMs and an arginine-glycine rich (RG-rich) LCD. We apply unbiased high-throughput biochemical approaches and identify critical RNA binding domains that confer specificity. We show that not all RRMs contribute equally to binding and find that RRM3, along with a downstream C-terminal charged region, are required for RNA binding. We find that HNRNPR also binds RNA G-quadrup"],"journal":["bioRxiv : the preprint server for biology"],"pagination":["2025.05.01.651718"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12247724"],"repository":["biostudies-literature"],"pubmed_title":["Contributions of Folded and Disordered Domains to RNA Binding by HNRNPR."],"pmcid":["PMC12247724"],"funding_grant_id":["R35 GM142864","T32 HL007149","T32 GM135095","T32 GM148376","T32 HL069768"],"pubmed_authors":["Martyr JG","Guzman BB","Hu Y","Cavazos FF","Goda GA","Dominguez D","Aleman MM","Jimenez A"],"additional_accession":[]},"is_claimable":false,"name":"Contributions of Folded and Disordered Domains to RNA Binding by HNRNPR.","description":"RNA binding proteins (RBPs) interact with and tightly regulate the fate of messenger RNAs but how RNA targets are recognized remains a challenging question. RBPs often contain multiple domains known to directly bind RNA, such as RNA recognition motifs (RRMs), as well as domains whose RNA binding capacity remains incompletely understood, <i>e.g.,</i> low complexity domains (LCDs). Here, we dissect HNRNPR, an RBP with three RRMs and an arginine-glycine rich (RG-rich) LCD. We apply unbiased high-throughput biochemical approaches and identify critical RNA binding domains that confer specificity. We show that not all RRMs contribute equally to binding and find that RRM3, along with a downstream C-terminal charged region, are required for RNA binding. We find that HNRNPR also binds RNA G-quadrup","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 May","modification":"2025-08-27T03:06:53.548Z","creation":"2025-08-27T03:06:53.548Z"},"accession":"S-EPMC12247724","cross_references":{"pubmed":["40654891"],"doi":["10.1101/2025.05.01.651718"]}}