Dedicated surveillance mechanism controls G-quadruplex forming non-coding RNAs in human mitochondria

Zbigniew Pietras, Magdalena A. Wojcik, Lukasz S. Borowski, Maciej Szewczyk, Tomasz M. Kulinski, Dominik Cysewski, Piotr P. Stepien, Andrzej Dziembowski () and Roman J. Szczesny ()
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Zbigniew Pietras: Laboratory of RNA Biology and Functional Genomics
Magdalena A. Wojcik: Laboratory of RNA Biology and Functional Genomics
Lukasz S. Borowski: Laboratory of RNA Biology and Functional Genomics
Maciej Szewczyk: Laboratory of RNA Biology and Functional Genomics
Tomasz M. Kulinski: Laboratory of RNA Biology and Functional Genomics
Dominik Cysewski: Laboratory of RNA Biology and Functional Genomics
Piotr P. Stepien: Laboratory of RNA Biology and Functional Genomics
Andrzej Dziembowski: Laboratory of RNA Biology and Functional Genomics
Roman J. Szczesny: Laboratory of RNA Biology and Functional Genomics

Nature Communications, 2018, vol. 9, issue 1, 1-15

Abstract: Abstract The GC skew in vertebrate mitochondrial genomes results in synthesis of RNAs that are prone to form G-quadruplexes (G4s). Such RNAs, although mostly non-coding, are transcribed at high rates and are degraded by an unknown mechanism. Here we describe a dedicated mechanism of degradation of G4-containing RNAs, which is based on cooperation between mitochondrial degradosome and quasi-RNA recognition motif (qRRM) protein GRSF1. This cooperation prevents accumulation of G4-containing transcripts in human mitochondria. In vitro reconstitution experiments show that GRSF1 promotes G4 melting that facilitates degradosome-mediated decay. Among degradosome and GRSF1 regulated transcripts we identified one that undergoes post-transcriptional modification. We show that GRSF1 proteins form a distinct qRRM group found only in vertebrates. The appearance of GRSF1 coincided with changes in the mitochondrial genome, which allows the emergence of G4-containing RNAs. We propose that GRSF1 appearance is an evolutionary adaptation enabling control of G4 RNA.

Date: 2018
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DOI: 10.1038/s41467-018-05007-9

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