2009
DOI: 10.1074/jbc.m109.055350
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Yeast AEP3p Is an Accessory Factor in Initiation of Mitochondrial Translation

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Cited by 22 publications
(34 citation statements)
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“…Simultaneous disruption of both FMT1 and AEP3 genes leads to a synthetic respiratory defect – a phenotype even more severe than that seen in fmt -deficient E. coli [23]. In vitro experiments have shown that complex formation between Aep3p and mIF2 promotes the binding of Met-tRNA i fMet – but not of fMet-tRNA i fMet – to mIF2, thus promoting Met-tRNA i fMet use in initiation.…”
Section: Mitochondrial Initiation Factor 2 (Mif2)mentioning
confidence: 99%
“…Simultaneous disruption of both FMT1 and AEP3 genes leads to a synthetic respiratory defect – a phenotype even more severe than that seen in fmt -deficient E. coli [23]. In vitro experiments have shown that complex formation between Aep3p and mIF2 promotes the binding of Met-tRNA i fMet – but not of fMet-tRNA i fMet – to mIF2, thus promoting Met-tRNA i fMet use in initiation.…”
Section: Mitochondrial Initiation Factor 2 (Mif2)mentioning
confidence: 99%
“…The ability of the yeast mitochondrial translational system to function without formylation of Met-tRNA is dependent on the presence of a factor designated Aep3p that is thought to interact with yeast IF2 mt and facilitates its use of Met-tRNA [57]. There is no clear homolog of this protein in mammals although it has a weak homology to the small subunit ribosomal protein MRPS27 (e = 9.3×10 −2 ).…”
Section: Initiation Of Protein Synthesis In Mammalian Mitochondriamentioning
confidence: 99%
“…Aep3 would allow the use of unformylated methionine as initiator amino acid by promoting the binding of unformylated Met-mt-tRNA to mt-IF2. 41 Whether this additional function is linked to the presence of the PPR motifs or rather to an additional domain of the protein has not yet been investigated.…”
Section: Principal Steps Of Mitochondrial Gene Expression Affected Bymentioning
confidence: 99%