{"doi":"10.1074/jbc.ra118.002291","title":"A low-complexity region in the YTH domain protein Mmi1 enhances RNA binding","abstract":null,"journal":"Journal of Biological Chemistry","year":2018,"id":614035,"datarank":0.4636563680037475,"base_score":3.091042453358316,"endowment":3.091042453358316,"self_citation_contribution":0.4636563680037475,"citation_network_contribution":0.0,"self_endowment_contribution":0.4636563680037475,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":21,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":1368763,"name":"Jane L. Wagstaff","orcid":null,"position":1,"is_corresponding":false},{"id":17828,"name":"Chris H. Hill","orcid":"0000-0001-7037-0611","position":2,"is_corresponding":false},{"id":1582132,"name":"Minmin Yu","orcid":null,"position":3,"is_corresponding":false},{"id":1379463,"name":"Stephen H. McLaughlin","orcid":"0000-0001-9135-6253","position":4,"is_corresponding":false},{"id":1368172,"name":"Stefan M.V. Freund","orcid":"0000-0002-7031-9872","position":5,"is_corresponding":false},{"id":592134,"name":"Lori A. Passmore","orcid":"0000-0003-1815-3710","position":6,"is_corresponding":false},{"id":1582129,"name":"James A.W. Stowell","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"A low-complexity region in the YTH domain protein Mmi1 enhances RNA binding","abstract":"that eliminates meiotic transcripts during normal vegetative growth. Mmi1 contains a YTH domain that binds specific RNA sequences, targeting mRNAs for degradation. The YTH domain of Mmi1 uses a noncanonical RNA-binding surface that includes contacts outside the conserved fold. Here, we report that an N-terminal extension that is proximal to the YTH domain enhances RNA binding. Using X-ray crystallography, NMR, and biophysical methods, we show that this low-complexity region becomes more ordered upon RNA binding. This enhances the affinity of the interaction of the Mmi1 YTH domain with specific RNAs by reducing the dissociation rate of the Mmi1-RNA complex. We propose that the low-complexity region influences RNA binding indirectly by reducing dynamic motions of the RNA-binding groove and stabilizing a conformation of the YTH domain that binds to RNA with high affinity. Taken together, our work reveals how a low-complexity region proximal to a conserved folded domain can adopt an ordered structure to aid nucleic acid binding.","is_dataset_classified":null,"base_score":3.091042453358316,"endowment":3.091042453358316,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"29695507","pmcid":"PMC6005420","openalex_id":"https://openalex.org/W2799789253","authors":[],"funders":[{"funder_name":"RCUK | Medical Research Council (MRC)","grant_id":"MC_U105192715","title":"Molecular mechanisms of mRNA polyadenylation and deadenylation"},{"funder_name":"EC | FP7 | FP7 Ideas: European Research Council (FP7 Ideas)","grant_id":"261151","title":"Macromolecular machines that regulate mRNA poly(A) tails: mechanisms of polyadenylation and deadenylation"}],"total_grants":2,"fwci":0.7424,"citation_percentile":0.68517696,"influential_citations":0,"citation_trend":[{"year":2019,"count":6},{"year":2020,"count":2},{"year":2021,"count":1},{"year":2022,"count":1},{"year":2023,"count":2},{"year":2024,"count":7},{"year":2025,"count":2}],"oa_status":"hybrid","license":"cc-by","oa_locations":[{"url":"http://www.jbc.org/article/S0021925820388943/pdf","host_type":"journal"},{"url":"http://www.jbc.org/article/S0021925820388943/pdf","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S0021925820388943?httpAccept=text/xml","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S0021925820388943?httpAccept=text/plain","host_type":"publisher"},{"url":"https://syndication.highwire.org/content/doi/10.1074/jbc.RA118.002291","host_type":"publisher"},{"url":"https://doi.org/10.1074/jbc.ra118.002291","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/29695507","host_type":"repository"},{"url":"http://europepmc.org/pmc/articles/PMC6005420","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/6005420","host_type":"repository"},{"url":"https://orcid.org/0000-0001-7037-0611>","host_type":"repository"},{"url":"https://eprints.whiterose.ac.uk/id/eprint/179531/1/1_s2.0_S0021925820388943_main.pdf","host_type":"repository"},{"url":"https://europepmc.org/articles/PMC6005420","host_type":"Europe_PMC"},{"url":"https://europepmc.org/articles/PMC6005420?pdf=render","host_type":"Europe_PMC"},{"url":"http://www.jbc.org/content/293/24/9210.full.pdf","host_type":""},{"url":"http://dx.doi.org/10.1074/jbc.RA118.002291","host_type":""},{"url":"https://eprints.whiterose.ac.uk/179531/1/1_s2.0_S0021925820388943_main.pdf","host_type":""},{"url":"https://epn-library.esrf.fr/flora/jsp/index_view_direct_anonymous.jsp?record=doc:PUB_ESRF:50122","host_type":""},{"url":"https://dx.doi.org/10.1074/jbc.ra118.002291","host_type":""},{"url":"https://eprints.whiterose.ac.uk/id/eprint/179531/","host_type":""}],"fields_of_study":["RNA Research and Splicing","RNA and protein synthesis mechanisms","RNA modifications and cancer","0301 basic medicine","0303 health sciences","03 medical and health sciences","Binding Sites","Crystallography, X-Ray","Models, Molecular","Protein Binding","Protein Conformation","Protein Domains","RNA, Fungal","RNA, Messenger","Schizosaccharomyces","Schizosaccharomyces pombe Proteins","Substrate Specificity","mRNA Cleavage and Polyadenylation Factors"],"mesh_terms":["Protein Domains","Binding Sites","Models, Molecular","Protein Binding","Protein Conformation","RNA, Fungal","RNA, Messenger","Schizosaccharomyces","Substrate Specificity","Crystallography, X-Ray","Schizosaccharomyces pombe Proteins","mRNA Cleavage and Polyadenylation Factors"],"keywords":["RNA","RNA-binding protein","Binding domain","Schizosaccharomyces pombe","Biology","Binding site","Biophysics","Cell biology","Biochemistry","Yeast","Saccharomyces cerevisiae","Gene","Meiosis","Intrinsically Disordered Protein","Mrna Decay","Deadenylation","Nuclear Magnetic Resonance (Nmr)","Yth Domain","Protein–nucleic Acid Interaction","Yt521-b Homology","Exosome Specificity Factor","Models, Molecular","mRNA Cleavage and Polyadenylation Factors","Crystallography","Binding Sites","Protein Conformation","Molecular","RNA, Fungal","Crystallography, X-Ray","Substrate Specificity","Schizosaccharomyces/chemistry","Protein Domains","Models","mRNA Cleavage and Polyadenylation Factors/chemistry","Schizosaccharomyces","X-Ray","Messenger/chemistry","RNA, Messenger","Schizosaccharomyces pombe Proteins","Schizosaccharomyces pombe Proteins/chemistry","Fungal/chemistry","Protein Binding"],"sdg_mappings":[{"sdg_number":0,"sdg_label":"Life in Land"}],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[{"name":"pdb"}],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-02T10:22:09.939903Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}