Pentatricopeptide repeat poly(A) binding protein KPAF4 stabilizes mitochondrial mRNAs in Trypanosoma brucei

Mikhail V. Mesitov, Tian Yu, Takuma Suematsu, Francois M. Sement, Liye Zhang, Clinton Yu, Lan Huang and Inna Aphasizheva ()
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Mikhail V. Mesitov: Boston University Medical Campus
Tian Yu: Boston University Medical Campus
Takuma Suematsu: Boston University Medical Campus
Francois M. Sement: Boston University Medical Campus
Liye Zhang: ShanghaiTechUniversity
Clinton Yu: University of California
Lan Huang: University of California
Inna Aphasizheva: Boston University Medical Campus

Nature Communications, 2019, vol. 10, issue 1, 1-15

Abstract: Abstract In Trypanosoma brucei, most mitochondrial mRNAs undergo editing, and 3′ adenylation and uridylation. The internal sequence changes and terminal extensions are coordinated: pre-editing addition of the short (A) tail protects the edited transcript against 3′-5′ degradation, while post-editing A/U-tailing renders mRNA competent for translation. Participation of a poly(A) binding protein (PABP) in coupling of editing and 3′ modification processes has been inferred, but its identity and mechanism of action remained elusive. We report identification of KPAF4, a pentatricopeptide repeat-containing PABP which sequesters the A-tail and impedes mRNA degradation. Conversely, KPAF4 inhibits uridylation of A-tailed transcripts and, therefore, premature A/U-tailing of partially-edited mRNAs. This quality check point likely prevents translation of incompletely edited mRNAs. We also find that RNA editing substrate binding complex (RESC) mediates the interaction between the 5′ end-bound pyrophosphohydrolase MERS1 and 3′ end-associated KPAF4 to enable mRNA circularization. This event appears to be critical for edited mRNA stability.

Date: 2019
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DOI: 10.1038/s41467-018-08137-2

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