A functional peptidyl-tRNA hydrolase, ICT1, has been recruited into the human mitochondrial ribosome

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A functional peptidyl-tRNA hydrolase, ICT1, has been recruited into the human mitochondrial ribosome

Bioinformatic analysis classifies the human protein encoded by immature colon carcinoma transcript-1 (ICT1) as one of a family of four putative mitochondrial translation release factors. However, this has not been supported by any experimental evidence. As only a single member of this family, mtRF1a, is required to terminate the synthesis of all 13 mitochondrially encoded polypeptides, the true...

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A functional peptidyl - tRNA hydrolase

Ricarda Richter, Joanna Rorbach, Aleksandra Pajak, Paul M Smith, Hans J Wessels, Martijn A Huynen, Jan A Smeitink, Robert N Lightowlers* and Zofia M Chrzanowska-Lightowlers* Mitochondrial Research Group, Institute for Ageing and Health, Medical School, Newcastle University, Newcastle upon Tyne, UK, Nijmegen Centre for Mitochondrial Disorders, Radboud University Nijmegen Medical Centre, Nijmegen...

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Peptidyl-tRNA hydrolase from Sulfolobus solfataricus.

An enzyme capable of liberating functional tRNA(Lys) from Escherichia coli diacetyl-lysyl-tRNA(Lys) was purified from the archae Sulfolobus solfataricus. Contrasting with the specificity of peptidyl- tRNA hydrolase (PTH) from E.coli, the S.solfataricus enzyme readily accepts E.coli formyl-methionyl-tRNA(fMet) as a substrate. N-terminal sequencing of this enzyme identifies a gene that has homolo...

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ICT1 comes to the rescue of mitochondrial ribosomes.

In the current issue, Richter et al (2010) show that mammalian mitochondrial ribosomes contain a ribosomal protein (ICT1) that acts as a ribosome-dependent, codonindependent peptidyl-tRNA hydrolase. This ribosomal protein can rescue ribosomes stalled on mRNAs lacking a termination codon. Every translational system runs into trouble when it encounters mRNAs that have lost the translation termina...

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Peptidyl-tRNA hydrolase and its critical role in protein biosynthesis.

Peptidyl-tRNA hydrolase (Pth) releases tRNA from peptidyl-tRNA by cleaving the ester bond between the peptide and the tRNA. Genetic analyses using Escherichia coli harbouring temperature-sensitive Pth have identified a number of translation factors involved in peptidyl-tRNA release. Accumulation of peptidyl-tRNA in the cells leads to depletion of aminoacyl-tRNA pools and halts protein biosynthe...

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ژورنال

عنوان ژورنال: The EMBO Journal

سال: 2010

ISSN: 0261-4189,1460-2075

DOI: 10.1038/emboj.2010.14