The Vsr-like protein FASTKD4 regulates the stability and polyadenylation of the MT-ND3 mRNA DOI Creative Commons
Xuan Yang, Maike Stentenbach, Laetitia A. Hughes

et al.

Nucleic Acids Research, Journal Year: 2024, Volume and Issue: unknown

Published: Dec. 27, 2024

Abstract Expression of the compact mitochondrial genome is regulated by nuclear encoded, mitochondrially localized RNA-binding proteins (RBPs). RBPs regulate lifecycles RNAs from transcription to degradation mediating RNA processing, maturation, stability and translation. The Fas-activated serine/threonine kinase (FASTK) family has been shown fine-tune discrete aspects gene expression. Although roles specific targets FASTK have elucidated, molecular mechanisms in metabolism remain unclear. Therefore, we resolved structure FASTKD4 at atomic level that includes RAP domain two FAST motifs, creating a positively charged cavity resembling very short patch repair endonuclease. Our biochemical studies show binds canonical poly(A) tail MT-ND3 enabling its maturation vitro role consistent with loss cells results decreased polyadenylation, which destabilizes this messenger mitochondria.

Language: Английский

The Vsr-like protein FASTKD4 regulates the stability and polyadenylation of the MT-ND3 mRNA DOI Creative Commons
Xuan Yang, Maike Stentenbach, Laetitia A. Hughes

et al.

Nucleic Acids Research, Journal Year: 2024, Volume and Issue: unknown

Published: Dec. 27, 2024

Abstract Expression of the compact mitochondrial genome is regulated by nuclear encoded, mitochondrially localized RNA-binding proteins (RBPs). RBPs regulate lifecycles RNAs from transcription to degradation mediating RNA processing, maturation, stability and translation. The Fas-activated serine/threonine kinase (FASTK) family has been shown fine-tune discrete aspects gene expression. Although roles specific targets FASTK have elucidated, molecular mechanisms in metabolism remain unclear. Therefore, we resolved structure FASTKD4 at atomic level that includes RAP domain two FAST motifs, creating a positively charged cavity resembling very short patch repair endonuclease. Our biochemical studies show binds canonical poly(A) tail MT-ND3 enabling its maturation vitro role consistent with loss cells results decreased polyadenylation, which destabilizes this messenger mitochondria.

Language: Английский

Citations

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