Journal
MOLECULAR CELL
Volume 72, Issue 4, Pages 727-+Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2018.10.010
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Funding
- Canadian Institutes of Health Research [366682]
- Fonds de recherche du Quebec - Sante (Chercheur-boursier Junior 2)
- NIH [R35GM128680]
- Canada Foundation for Innovation
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [T32GM007445, R35GM128680] Funding Source: NIH RePORTER
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mRNAs form ribonucleoprotein complexes (mRNPs) by association with proteins that are crucial for mRNA metabolism. While the mRNP proteome has been well characterized, little is known about mRNP organization. Using a single-molecule approach, we show that mRNA conformation changes depending on its cellular localization and translational state. Compared to nuclear mRNPs and lncRNPs, association with ribosomes decompacts individual mRNAs, while pharmacologically dissociating ribosomes or sequestering them into stress granules leads to increased compaction. Moreover, translating mRNAs rarely show co-localized 5 0 and 3 0 ends, indicating either that mRNAs are not translated in a closed-loop configuration, or that mRNA circularization is transient, suggesting that a stable closed-loop conformation is not a universal state for all translating mRNAs.
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