Crystal structure of dimeric human PNPase reveals why disease-linked mutants suffer from low RNA import and degradation activities

Author:

Golzarroshan Bagher123,Lin Chia-Liang1,Li Chia-Lung1,Yang Wei-Zen1,Chu Lee-Ya123,Agrawal Sashank145,Yuan Hanna S124

Affiliation:

1. Institute of Molecular Biology, Academia Sinica, Taipei, Taiwan 11529, Republic of China

2. Chemical Biology and Molecular Biophysics Program, Taiwan International Graduate Program, Academia Sinica, Taipei, Taiwan 11529, Republic of China

3. Institute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu, Taiwan 30013, Republic of China

4. Molecular and Cell Biology Program, Taiwan International Graduate Program, Academia Sinica, Taipei, Taiwan 11529, Republic of China

5. Graduate Institute of Life Sciences, National Defense Medical Center, Taipei, Taiwan 11490, Republic of China

Publisher

Oxford University Press (OUP)

Subject

Genetics

Reference43 articles.

1. Mitochondrial machineries for protein import and assembly;Wiedemann;Annu. Rev. Biochem.,2017

2. Evolution of macromolecular import pathways in mitochondria, hydrogenosomes and mitosomes;Lithgow;Phil. Trans. R. Soc. B,2010

3. Mitochondrial noncoding RNA transport;Kim;BMB Rep.,2017

4. PNPASE and RNA trafficking into mitochondria;Wang;Biochim. Biophys. Acta Gene Reg. Mech.,2012

5. PNPASE regulates RNA import into mitochondria;Wang;Mol. Cell,2010

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