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Toward a Systems View on RNA-binding Proteins and Associated RNAs in Plants: Guilt by Association

Overview
Journal Plant Cell
Specialties Biology
Cell Biology
Date 2022 Dec 3
PMID 36461946
Authors
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Abstract

RNA-binding proteins (RBPs) have a broad impact on most biochemical, physiological, and developmental processes in a plant's life. RBPs engage in an on-off relationship with their RNA partners, accompanying virtually every stage in RNA processing and function. While the function of a plethora of RBPs in plant development and stress responses has been described, we are lacking a systems-level understanding of components in RNA-based regulation. Novel techniques have substantially enlarged the compendium of proteins with experimental evidence for binding to RNAs in the cell, the RNA-binding proteome. Furthermore, ribonomics methods have been adapted for use in plants to profile the in vivo binding repertoire of RBPs genome-wide. Here, we discuss how recent technological achievements have provided novel insights into the mode of action of plant RBPs at a genome-wide scale. Furthermore, we touch upon two emerging topics, the connection of RBPs to phase separation in the cell and to extracellular RNAs. Finally, we define open questions to be addressed to move toward an integrated understanding of RBP function.

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References
1.
Yang Y, Di C, Hu B, Zhou M, Liu Y, Song N . CLIPdb: a CLIP-seq database for protein-RNA interactions. BMC Genomics. 2015; 16:51. PMC: 4326514. DOI: 10.1186/s12864-015-1273-2. View

2.
Hilson P, Carroll K, Masson P . Molecular characterization of PAB2, a member of the multigene family coding for poly(A)-binding proteins in Arabidopsis thaliana. Plant Physiol. 1993; 103(2):525-33. PMC: 159012. DOI: 10.1104/pp.103.2.525. View

3.
SIMPSON G, Clark G, Rothnie H, Boelens W, Van Venrooij W, Brown J . Molecular characterization of the spliceosomal proteins U1A and U2B" from higher plants. EMBO J. 1995; 14(18):4540-50. PMC: 394546. DOI: 10.1002/j.1460-2075.1995.tb00133.x. View

4.
Quesada V, Macknight R, Dean C, Simpson G . Autoregulation of FCA pre-mRNA processing controls Arabidopsis flowering time. EMBO J. 2003; 22(12):3142-52. PMC: 162157. DOI: 10.1093/emboj/cdg305. View

5.
Kramer K, Sachsenberg T, Beckmann B, Qamar S, Boon K, Hentze M . Photo-cross-linking and high-resolution mass spectrometry for assignment of RNA-binding sites in RNA-binding proteins. Nat Methods. 2014; 11(10):1064-70. PMC: 6485471. DOI: 10.1038/nmeth.3092. View