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

被引：14
作者：
Brizio, C
Barile, M
Brandsch, R
机构：
[1] Univ Bari, Dipartimento Biochim & Biol Mol, I-70126 Bari, Italy
[2] CNR, Ctr Studio Mitocondri & Metab Energet, I-70126 Bari, Italy
来源：
FEBS LETTERS | 2002年 / 522卷 / 1-3期
关键词：
dimethylglycine dehydrogenase; flavinylation; flavinylation stimulating factor; mitochondrion; precursor processing;
D O I：
10.1016/S0014-5793(02)02927-7
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The flavinylation and the presequence processing of the mitochondrial matrix enzyme dimethylglycine dehydrogenase (Me(2)GlyDH) were investigated with the reticulocyte lysate translated precursor (pMe(2)GlyDH) added to solubilised mitoplasts of rat liver mitochondria. The flavinylation of PMe(2)GlyDH was strictly dependent on the addition of mitochondrial protein(s), among which the mitochondrial flavinylation stimulating factor [Brizio C., et A. (2000) Eur. J. Biochem 267, 4346-4354], that actively promotes holo-Me(2)GlyDH 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 pMe(2)GlyDH demonstrated that the covalent attachment of the flavin moiety preceded the presequence processing by mitochondrial processing peptidase. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
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页码：141 / 146
页数：6
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