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Targeting of the cytosolic poly(A) binding protein PABPC1 to mitochondria causes mitochondrial translation inhibition

Lookup NU author(s): Dr Mateusz Wydro, Agnieszka Bobrowicz, Dr Richard Temperley, Professor Robert Lightowlers, Professor Zofia Chrzanowska-LightowlersORCiD



Mammalian mitochondria contain their own genome that is almost fully transcribed from both strands, generating polycistronic RNA units that are processed and matured. The mitochondrial mRNA is modified by oligo- or polyadenylation at the 3' termini, but the exact function of this post-transcriptional addition is unclear. Current debate focuses on the role of polyadenylation in transcript stability. An equally likely function that has received little attention is that, as in the cytosol of eukaryotes, polyadenylation facilitates translation in the mitochondrion. To address this issue, we have targeted cytosolic proteins to the mitochondrion, a poly(A) specific 3' exoribonuclease, mtPARN, and a poly(A)binding protein, mtPABP1. Removal of the 3' adenylyl extensions had a variable effect on mt-mRNA steady-state levels, increasing (MTND1, 2, 5) or decreasing (MTCO1, 2, RNA14) certain species with minimal effect on others (RNA7, MTND3). Translation was markedly affected, but interpretation of this was complicated by the concomitant 3' truncation of the open reading frame in most cases. Coating of the poly(A) tail by mtPABP1, however, did not lead to transcript decay but caused a marked inhibition of mitochondrial translation. These data are consistent with endogenous RNA-binding factor(s) interacting with the poly(A) to optimize mitochondrial protein synthesis.

Publication metadata

Author(s): Wydro M, Bobrowicz A, Temperley RJ, Lightowlers RN, Chrzanowska-Lightowlers ZM

Publication type: Article

Publication status: Published

Journal: Nucleic Acids Research

Year: 2010

Volume: 38

Issue: 11

Pages: 3732-3742

Print publication date: 09/02/2010

Date deposited: 06/09/2010

ISSN (print): 0305-1048

ISSN (electronic): 1362-4962

Publisher: Oxford University Press


DOI: 10.1093/nar/gkq068


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Funder referenceFunder name
074454/Z/04/ZWellcome Trust
BB/F011520/1Biotechnology and Biological Sciences Research Council