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Structural basis for guide RNA selection by the RESC1-RESC2 complex.

Luciano G Dolce¹, Yevheniia Nesterenko¹, Leon Walther¹

¹EMBL Grenoble, 71 Avenue des Martyrs, 38042 Grenoble, France.

Nucleic Acids Research

|March 31, 2023

Summary

This summary is machine-generated.

Kinetoplastid parasites use RNA editing to create functional transcripts. The RESC complex structure reveals RESC2 binds guide RNAs, crucial for this process and potential drug targets.

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Area of Science:

Molecular Biology
Parasitology
Structural Biology

Background:

Kinetoplastid parasites depend on RNA-templated RNA editing for mitochondrial gene expression.
The 20-subunit RNA editing substrate binding complex (RESC) orchestrates RNA editing but its structure and function are poorly understood.
Previous studies lacked molecular structures and biochemical data on purified RESC components.

Purpose of the Study:

To determine the cryo-EM structure of the RESC1-RESC2 module, a key part of the RESC complex.
To elucidate the structural basis for guide RNA (gRNA) binding within the RESC complex.
To provide insights into the assembly and function of RNA editing machinery in kinetoplastids.

Main Methods:

Cryo-electron microscopy (cryo-EM) was used to determine the structure of the Trypanosoma brucei RESC1-RESC2 complex.
Structural analysis was performed to compare RESC1 and RESC2 subunits and identify RNA-binding sites.
Biochemical assays were implied to assess the binding of nucleosides to RESC subunits.

Main Results:

The cryo-EM structure revealed RESC1 and RESC2 form an obligatory domain-swapped dimer.
Both RESC1 and RESC2 subunits share similar tertiary structures.
Only the RESC2 subunit selectively binds 5'-triphosphate-nucleosides, characteristic of gRNAs.

Conclusions:

RESC2 is proposed as the primary 5'-end binding site for guide RNAs within the RESC complex.
The structure provides a foundation for understanding larger RNA-editing modules in kinetoplastids.
This structural information may aid in the development of novel anti-parasitic drugs.