TRBP ensures efficient Dicer processing of precursor microRNA in RNA-crowded environments

Journal Article (2016)
Author(s)

Mohamed Fareh (TU Delft - BN/Chirlmin Joo Lab, Kavli institute of nanoscience Delft)

Kyu Hyeon Yeom (TU Delft - BN/Chirlmin Joo Lab, Kavli institute of nanoscience Delft)

Anna C. Haagsma (Kavli institute of nanoscience Delft, TU Delft - BN/Technici en Analisten)

S. Chauhan (TU Delft - BN/Chirlmin Joo Lab, Kavli institute of nanoscience Delft)

Inha Heo (Kavli institute of nanoscience Delft, TU Delft - BN/Chirlmin Joo Lab)

C. Joo (Kavli institute of nanoscience Delft, TU Delft - BN/Chirlmin Joo Lab)

Research Group
BN/Chirlmin Joo Lab
Copyright
© 2016 M. Fareh, K.H. Yeom, A.C. van Eijkeren-Haagsma, S. Chauhan, I. Heo, C. Joo
DOI related publication
https://doi.org/10.1038/ncomms13694
More Info
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Publication Year
2016
Language
English
Copyright
© 2016 M. Fareh, K.H. Yeom, A.C. van Eijkeren-Haagsma, S. Chauhan, I. Heo, C. Joo
Research Group
BN/Chirlmin Joo Lab
Volume number
7
Pages (from-to)
1-11
Reuse Rights

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Abstract

The RNA-binding protein TRBP is a central component of the Dicer complex. Despite a decade of biochemical and structural studies, the essential functionality of TRBP in microRNA (miRNA) biogenesis remains unknown. Here we show that TRBP is an integral cofactor for time-efficient Dicer processing in RNA-crowded environments. We competed for Dicer processing of pre-miRNA with a large amount of cellular RNA species and found that Dicer-TRBP, but not Dicer alone, remains resilient. To apprehend the mechanism of this substrate selectivity, we use single-molecule fluorescence. The real-time observation reveals that TRBP acts as a gatekeeper, precluding Dicer from engaging with pre-miRNA-like substrates. TRBP acquires the selectivity using the PAZ domain of Dicer, whereas Dicer moderates the RNA-binding affinity of TRBP for fast turnover. This coordinated action between TRBP and Dicer accomplishes an efficient way of discarding pre-miRNA-like substrates.

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