MTERF3, the most conserved member of the mTERF-family, is a modular factor involved in mitochondrial protein synthesis (Articolo in rivista)

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Label
  • MTERF3, the most conserved member of the mTERF-family, is a modular factor involved in mitochondrial protein synthesis (Articolo in rivista) (literal)
Anno
  • 2006-01-01T00:00:00+01:00 (literal)
Alternative label
  • Roberti M, Bruni F, Loguercio Polosa P, Manzari C, Gadaleta MN, Cantatore P. (2006)
    MTERF3, the most conserved member of the mTERF-family, is a modular factor involved in mitochondrial protein synthesis
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Roberti M, Bruni F, Loguercio Polosa P, Manzari C, Gadaleta MN, Cantatore P. (literal)
Pagina inizio
  • 1199 (literal)
Pagina fine
  • 1206 (literal)
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  • 1757 (literal)
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  • Pubblicazione internazionale di interesse scientifico (literal)
Note
  • ISI Web of Science (WOS) (literal)
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  • Dipartimento di Biochimica e Biologia Molecolare \"Ernesto Quagliariello\", Universita di Bari, Via Orabona 4, 70125 Bari, Italy Istituto di Biomembrane e Bioenergetica-CNR, via Amendola 165/A, 70126 Bari, Italy (literal)
Titolo
  • MTERF3, the most conserved member of the mTERF-family, is a modular factor involved in mitochondrial protein synthesis (literal)
Abstract
  • The MTERF-family is a wide family of proteins identified in Metazoa and plants which includes the known mitochondrial transcription termination factors. With the aim to shed light on the function of MTERF-family members in Drosophila, we performed the cloning and characterization of D-MTERF3, a component of the most conserved group of this family. D-MTERF3 is a mitochondrial protein of 323 amino acids. Sequence analysis in seven different organisms showed that the protein contains five conserved \"mTERF-motifs\", three of which include a leucine zipper-like domain. D-MTERF3 knock-down, obtained by RNAi in D.Mel-2 cells, did not affect mitochondrial replication and transcription. On the contrary, it decreased to a variable extent the rate of labelling of about half of the mitochondrial polypeptides, with ND1 being the most affected by D-MTERF3 depletion. These results indicate that D-MTERF3 is involved in mitochondrial translation. This role, likely based on protein-protein interactions, may be exerted either through a direct interaction with the translation machinery or by bridging the mitochondrial transcription and translation apparatus. (literal)
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