Rescuing stalled mammalian mitoribosomes - what can we learn from bacteria?

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ID: 76104
2020
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Abstract
In the canonical process of translation, newly completed proteins escape from the ribosome following cleavage of the ester bond that anchors the polypeptide to the P-site tRNA, after which the ribosome can be recycled to initiate a new round of translation. Not all protein synthesis runs to completion as various factors can impede the progression of ribosomes. Rescuing of stalled ribosomes in mammalian mitochondria, however, does not share the same mechanisms that many bacteria use. The classic method for rescuing bacterial ribosomes is -translation. The key components of this system are absent from mammalian mitochondria; however, four members of a translation termination factor family are present, with some evidence of homology to members of a bacterial back-up rescue system. To date, there is no definitive demonstration of any other member of this family functioning in mitoribosome rescue. Here, we provide an overview of the processes and key players of canonical translation termination in both bacteria and mammalian mitochondria, followed by a perspective of the bacterial systems used to rescue stalled ribosomes. We highlight any similarities or differences with the mitochondrial translation release factors, and suggest potential roles for these proteins in ribosome rescue in mammalian mitochondria.
Reference Key
ayyub2020rescuingjournal Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Ayyub, Shreya Ahana;Gao, Fei;Lightowlers, Robert N;Chrzanowska-Lightowlers, Zofia M;
Journal journal of cell science
Year 2020
DOI
jcs231811
URL
Keywords
arfa arfb arft c12orf65 ict1 mammalian mitochondria mitoribosomes mtrf1 release factor stalled ribosome trans-translation translation termination

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