To gain further information on the role of mitochondrial transcription factor A (TFAM) in mitochondrial biogenesis, we studied the post-translational modifications of the protein in 6- and 28-month-old rat liver. Mass spectrometry and immunoblot analysis revealed that TFAM was acetylated at a single lysine residue and that the level of acetylation did not change with age. The measurement of the content of TFAM and of mitochondrial DNA (mtDNA) in several organs (cerebellum, heart, kidney, and liver) of young and old rats showed an age-related increase of mtDNA and TFAM in all the organs analyzed, except in heart. These data are discussed in the light of the multiple roles of TFAM in mitochondrial biogenesis and of the age-related change of the mitochondrial transcription.

Acetylation and level of mitochondrial transcription factor A in several organs of young and old rats.

Musicco C;
2003

Abstract

To gain further information on the role of mitochondrial transcription factor A (TFAM) in mitochondrial biogenesis, we studied the post-translational modifications of the protein in 6- and 28-month-old rat liver. Mass spectrometry and immunoblot analysis revealed that TFAM was acetylated at a single lysine residue and that the level of acetylation did not change with age. The measurement of the content of TFAM and of mitochondrial DNA (mtDNA) in several organs (cerebellum, heart, kidney, and liver) of young and old rats showed an age-related increase of mtDNA and TFAM in all the organs analyzed, except in heart. These data are discussed in the light of the multiple roles of TFAM in mitochondrial biogenesis and of the age-related change of the mitochondrial transcription.
2003
Istituto di Biomembrane, Bioenergetica e Biotecnologie Molecolari (IBIOM)
301
187
191
mtDNA
Copy number
TFAM
Acetylation
Aging
Impact factor 2,935 Il fattore di trascrizione mitocondriale A (TFAM) è necessario per il mantenimento del DNA mitocondriale e insieme ad altri fattori ne stimola la trascrizione. L’acetilazione di TFAM, probabilmente a livello di un singolo residuo di lisina, è la prima modificazione post-traduzionale riportata per una DNA-binding protein mitocondriale. Dato che TFAM agisce come una proteina histone-like, la sua acetilazione potrebbe essere coinvolta nella regolazione del legame della proteina al DNA, dei cambiamenti conformazionali del DNA o delle interazioni con le altre proteine dell’apparato di replicazione e trascrizione mitocondriale.
7
info:eu-repo/semantics/article
262
Dinardo, Mm; Musicco, C; Fracasso, F; Milella, F; Gadaleta, Mn; Gadaleta, G; Cantatore, P
01 Contributo su Rivista::01.01 Articolo in rivista
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/20.500.14243/454528
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