title: A family of RRM-type RNA-binding proteins specific to plant mitochondria.
abstract: Expression of higher plant mitochondrial (mt) genes is regulated at the transcriptional, posttranscriptional, and translational levels, but the vast majority of the mtDNA and RNA-binding proteins involved remain to be identified. Plant mt single-stranded nucleic acid-binding proteins were purified by affinity chromatography, and corresponding genes have been identified. A majority of these proteins belong to a family of RNA-binding proteins characterized by the presence of an N-terminal RNA-recognition motif (RRM) sequence. They diverge in their C-terminal sequences, suggesting that they can be involved in different plant mt regulation processes. Mitochondrial localization of the proteins was confirmed both in vitro and in vivo and by immunolocalization. Binding experiments showed that several proteins have a preference for poly(U)-rich sequences. This mt protein family contains the ubiquitous RRM motif and has no known mt counterpart in non-plant species. Phylogenetic and functional analysis suggest a common ancestor with RNA-binding glycine-rich proteins (GRP), a family of developmentally regulated proteins of unknown function. As with several plant, cyanobacteria, and animal proteins that have similar structures, the expression of one of the Arabidopsis thaliana mt RNA-binding protein genes is induced by low temperatures.
authors.affiliation: Institut de Biologie Moléculaire des Plantes du Centre National de la Recherche Scientifique, 12 rue du général Zimmer, 67084 Strasbourg, France.
authors.forename: Matthieu
authors.initials: M
authors.lastname: Vermel
authors.forename: Benoit
authors.initials: B
authors.lastname: Guermann
authors.forename: Ludovic
authors.initials: L
authors.lastname: Delage
authors.forename: Jean-Michel
authors.initials: JM
authors.lastname: Grienenberger
authors.forename: Laurence
authors.initials: L
authors.lastname: Maréchal-Drouard
authors.forename: José M
authors.initials: JM
authors.lastname: Gualberto
mesh_terms: D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D017360:Arabidopsis; D015152:Blotting, Northern; D003080:Cold Temperature; D018076:DNA, Complementary / Q000378:metabolism; D004277:DNA, Single-Stranded; D003902:Detergents / Q000494:pharmacology; D008928:Mitochondria / Q000378:metabolism*; D008969:Molecular Sequence Data; D009696:Nucleic Acids / Q000378:metabolism; D017830:Octoxynol / Q000494:pharmacology; D010802:Phylogeny; D010940:Plant Proteins / Q000378:metabolism*; D010944:Plants / Q000378:metabolism; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D012313:RNA / Q000378:metabolism*; D016601:RNA-Binding Proteins; D020133:Reverse Transcriptase Polymerase Chain Reaction; D012262:Ribonucleoside Diphosphate Reductase; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid; D011198:Solanum tuberosum / Q000235:genetics; D013696:Temperature; D014026:Nicotiana / Q000235:genetics; D025521:Tumor Suppressor Proteins / Q000378:metabolism
chemical_list: D018076:DNA, Complementary; D004277:DNA, Single-Stranded; D003902:Detergents; D009696:Nucleic Acids; D010940:Plant Proteins; D016601:RNA-Binding Proteins; C117851:RRM1 protein, Trypanosoma brucei; D025521:Tumor Suppressor Proteins; D012313:RNA; D017830:Octoxynol; C475286:RRM1 protein, human; D012262:Ribonucleoside Diphosphate Reductase