{"doi":"10.1111/ppl.12286","title":"The evolutionarily conserved multifunctional glycine‐rich <scp>RNA</scp>‐binding proteins play key roles in development and stress adaptation","abstract":"<jats:p>The class <jats:styled-content style=\"fixed-case\">IV</jats:styled-content> glycine‐rich <jats:styled-content style=\"fixed-case\">RNA</jats:styled-content>‐binding proteins are a distinct subgroup within the heterogenous superfamily of glycine‐rich proteins (<jats:styled-content style=\"fixed-case\">GRPs</jats:styled-content>). They are distinguished by the presence of an <jats:styled-content style=\"fixed-case\">RNA</jats:styled-content>‐binding domain in the N‐terminus; generally in the form of an <jats:styled-content style=\"fixed-case\">RNA</jats:styled-content>‐recognition motif (<jats:styled-content style=\"fixed-case\">RRM</jats:styled-content>) or a cold‐shock domain (<jats:styled-content style=\"fixed-case\">CSD</jats:styled-content>). These are followed by a C‐terminal glycine‐rich domain. Growing evidence suggests that these proteins play key roles in the adaptation of organisms to biotic and abiotic stresses including those resulting from pathogenesis, alterations in the osmotic, saline and oxidative environment and changes in temperature. Similar vertebrate proteins are also cold‐induced and involved in, e.g. hibernation, suggesting evolutionarily conserved functions. The class <jats:styled-content style=\"fixed-case\">IV RNA</jats:styled-content>‐binding <jats:styled-content style=\"fixed-case\">GRPs</jats:styled-content> are likely to operate as key molecular components of hormonally regulated development and to work by regulating gene expression at multiple levels by modifying alternative splicing, <jats:styled-content style=\"fixed-case\">mRNA</jats:styled-content> export, <jats:styled-content style=\"fixed-case\">mRNA</jats:styled-content> translation and <jats:styled-content style=\"fixed-case\">mRNA</jats:styled-content> degradation.</jats:p>","journal":"Physiologia Plantarum","year":2015,"id":682144,"datarank":0.6716005221717312,"base_score":4.477336814478207,"endowment":4.477336814478207,"self_citation_contribution":0.6716005221717312,"citation_network_contribution":0.0,"self_endowment_contribution":0.6716005221717312,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":87,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":18,"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":1782124,"name":"John Hancock","orcid":null,"position":1,"is_corresponding":false},{"id":1782125,"name":"Doru Pamfil","orcid":null,"position":2,"is_corresponding":false},{"id":1472642,"name":"Ian Wilson","orcid":"0000-0001-7303-164X","position":3,"is_corresponding":false},{"id":1782129,"name":"Michael Ladomery","orcid":null,"position":4,"is_corresponding":false},{"id":1782123,"name":"Oana Ciuzan","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"The evolutionarily conserved multifunctional glycine‐rich <scp>RNA</scp>‐binding proteins play key roles in development and stress adaptation","abstract":"<jats:p>The class <jats:styled-content style=\"fixed-case\">IV</jats:styled-content> glycine‐rich <jats:styled-content style=\"fixed-case\">RNA</jats:styled-content>‐binding proteins are a distinct subgroup within the heterogenous superfamily of glycine‐rich proteins (<jats:styled-content style=\"fixed-case\">GRPs</jats:styled-content>). They are distinguished by the presence of an <jats:styled-content style=\"fixed-case\">RNA</jats:styled-content>‐binding domain in the N‐terminus; generally in the form of an <jats:styled-content style=\"fixed-case\">RNA</jats:styled-content>‐recognition motif (<jats:styled-content style=\"fixed-case\">RRM</jats:styled-content>) or a cold‐shock domain (<jats:styled-content style=\"fixed-case\">CSD</jats:styled-content>). These are followed by a C‐terminal glycine‐rich domain. Growing evidence suggests that these proteins play key roles in the adaptation of organisms to biotic and abiotic stresses including those resulting from pathogenesis, alterations in the osmotic, saline and oxidative environment and changes in temperature. Similar vertebrate proteins are also cold‐induced and involved in, e.g. hibernation, suggesting evolutionarily conserved functions. The class <jats:styled-content style=\"fixed-case\">IV RNA</jats:styled-content>‐binding <jats:styled-content style=\"fixed-case\">GRPs</jats:styled-content> are likely to operate as key molecular components of hormonally regulated development and to work by regulating gene expression at multiple levels by modifying alternative splicing, <jats:styled-content style=\"fixed-case\">mRNA</jats:styled-content> export, <jats:styled-content style=\"fixed-case\">mRNA</jats:styled-content> translation and <jats:styled-content style=\"fixed-case\">mRNA</jats:styled-content> degradation.</jats:p>","is_dataset_classified":null,"base_score":4.477336814478207,"endowment":4.477336814478207,"datacite_reuse_total":18,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"25243592","pmcid":null,"openalex_id":"https://openalex.org/W2026250350","authors":[],"funders":[{"funder_name":"Deutsche Bundesstiftung Umwelt","grant_id":"awarded to Oana 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