Flavinylation of the precursor of mitochondrial dimethylglycine dehydrogenase by intact and solubilised mitochondria

FEBS Letters

Brizio, Carmen²  Brandsch, Roderich¹  Barile, Maria² 

[1]Institut für Biochemie und Molekularbiologie, Universität Freiburg, Hermann-Herder-Str. 7, 79104 Freiburg, Germany

[2]Dipartimento di Biochimica e Biologia Molecolare, Università di Bari, and Centro di Studio sui Mitocondri e Metabolismo Energetico, C.N.R., Via Orabona 4, 70126 Bari, Italy

关键词: Dimethylglycine dehydrogenase;    Flavinylation;    Flavinylation stimulating factor;    Mitochondrion;    Precursor processing;    FCCP;    carbonylcyanide p-trifluoromethoxyphenylhydrazone;    Me2GlyDH;    dimethylglycine dehydrogenase;    mMe2GlyDH;    mature form of Me2GlyDH;    MPP;    mitochondrial processing peptidase;    mtFSF;    mitochondrial flavinylation stimulating factor;    pMe2GlyDH;    precursor form of Me2GlyDH;    RL;    reticulocyte lysate;    RLM;    rat liver mitochondria;    SDH;    succinate dehydrogenase;   

DOI  :  10.1016/S0014-5793(02)02927-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The flavinylation and the presequence processing of the mitochondrial matrix enzyme dimethylglycine dehydrogenase (Me₂GlyDH) were investigated with the reticulocyte lysate translated precursor (pMe₂GlyDH) added to solubilised mitoplasts of rat liver mitochondria. The flavinylation of pMe₂GlyDH was strictly dependent on the addition of mitochondrial protein(s), among which the mitochondrial flavinylation stimulating factor [Brizio C., et al. (2000) Eur. J. Biochem 267, 4346–4354], that actively promotes holo-Me₂GlyDH formation. The precursor processing, that accompanies the biogenesis of the enzyme, was not required to allow the flavinylation to proceed. The comparison of the time course of the flavinylation and the processing of pMe₂GlyDH demonstrated that the covalent attachment of the flavin moiety preceded the presequence processing by mitochondrial processing peptidase.

【 授权许可】

Unknown