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- Title
Flavinylation of the precursor of mitochondrial dimethylglycine dehydrogenase by intact and solubilised mitochondria
- Authors
Brizio, Carmen; Barile, Maria; Brandsch, Roderich
- Abstract
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.
- Subjects
MITOCHONDRIA; DEHYDROGENASES; FLAVINS
- Publication
FEBS Letters, 2002, Vol 522, Issue 1-3, p141
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/S0014-5793(02)02927-7