The landscape of eukaryotic mRNPs
- Department of Biochemistry and Howard Hughes Medical Institute, University of Colorado Boulder, Boulder, Colorado 80303, USA
- Corresponding author: roy.parker{at}colorado.edu
Abstract
The proper regulation of mRNA processing, localization, translation, and degradation occurs on mRNPs. However, the global principles of mRNP organization are poorly understood. We utilize the limited, but existing, information available to present a speculative synthesis of mRNP organization with the following key points. First, mRNPs form a compacted structure due to the inherent folding of RNA. Second, the ribosome is the principal mechanism by which mRNA regions are partially decompacted. Third, mRNPs are 50%–80% protein by weight, consistent with proteins modulating mRNP organization, but also suggesting the majority of mRNA sequences are not directly interacting with RNA-binding proteins. Finally, the ratio of mRNA-binding proteins to mRNAs is higher in the nucleus to allow effective RNA processing and limit the potential for nuclear RNA based aggregation. This synthesis of mRNP understanding provides a model for mRNP biogenesis, structure, and regulation with multiple implications.
Footnotes
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Abbreviations: EM, electron microscope; hnRNP, heterogeneous ribonucleoprotein particle; kDa, kilodaltons; MD, molecular dynamics; MFC, multifactor complex; mRNP, messenger ribonucleprotein; MW, molecular weight; ncRNA, noncoding RNA; RNA-BP, RNA-binding protein; rRNA, ribosomal RNA; SAXS, small-angle X-ray scattering; smFISH, single-molecule FISH; snoRNAs, small nucleolar RNA; snRNAs, small nuclear RNA; UTR, untranslated region
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Article is online at http://www.rnajournal.org/cgi/doi/10.1261/rna.073601.119.
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