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Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
Published on: September 23, 2021
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mRNA interactions with disordered regions control protein activity
Yang Luo1, Supriya Pratihar2, Ellen H Horste1,3
1Cancer Biology and Genetics Program, Sloan Kettering Institute, New York, NY 10065, USA.
Biorxiv : the Preprint Server for Biology
|February 24, 2023
Summary
Messenger RNAs (mRNAs) within specific cytoplasmic compartments, such as TIS granules (TGs), control protein complex formation. This study reveals that mRNAs act as chaperones, guiding intrinsically disordered regions (IDRs) for novel protein regulation.
Area of Science:
- Molecular Biology
- Cell Biology
- Biochemistry
Background:
- Cytoplasmic compartmentalization influences protein translation and function.
- Messenger RNAs (mRNAs) localize to specific compartments like TIS granules (TGs) via their 3'UTRs.
- Transcription factors, including MYC, are translated in TGs, enabling unique protein complex formation.
Approach:
- Investigated the mechanism by which TG translation facilitates protein complex assembly.
- Identified that MYC protein complexes involving its intrinsically disordered region (IDR) form exclusively during TG translation.
- Discovered that TG-enriched mRNAs bind to a novel RNA-binding domain within IDRs of transcription factors.
Key Points:
- TG-dependent protein complex assembly requires specific TG-enriched mRNAs.
- mRNA-IDR interactions alter the conformational ensemble of IDRs, promoting complex formation.
- This mechanism allows for the formation of MYC protein complexes with distinct nuclear functions.
Conclusions:
- Certain mRNAs possess IDR chaperone activity, regulating protein conformations.
- Identified a novel mode of protein activity regulation beyond post-translational modifications.
- mRNA-dependent control of protein functional states is suggested to be widespread due to prevalent RNA-IDR interactions.
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