A protein factor of rat liver mitochondrial matrix involved in flavinylation of dimethylglycine dehydrogenase.
作者： Carmen Brizio , Annegret Otto , Roderich Brandsch , Salvatore Passarella , Maria Barile
DOI: 10.1046/J.1432-1327.2000.01464.X
关键词:
摘要: The involvement of rat liver mitochondria in the flavinylation mitochondrial matrix flavoenzyme dimethylglycine dehydrogenase (Me2GlyDH) has been investigated. Me2GlyDH was synthesized as an apoenzyme rabbit reticulocyte lysate (RL) transcription/translation system and its monitored by virtue trypsin resistance holoenzyme. rate holoenzyme formation presence FAD stimulated with increasing efficiency addition solubilized mitoplasts, DEAE-purified fraction. Apo-Me2GlyDH also converted into when mitoplasts were supplemented FMN ATP. This observation is consistent existence a synthetase generating needed for from precursors. Holoenzyme increased linearly concentration protein assay, depended on amount externally added saturation characteristics. These findings suggest factor which stimulates flavinylation. different both heat shock (Hsp)70, shown immunodepletion experiments, Hsp60, demonstrated capability fraction devoid Hsp60 to accelerate RL translated purified Me2GlyDH.
core.ac.uk
sci-hub.se 参考文章(34)
T. Saijo, W.J. Welch, K. Tanaka, Intramitochondrial folding and assembly of medium-chain acyl-CoA dehydrogenase (MCAD). Demonstration of impaired transfer of K304E-variant MCAD from its complex with hsp60 to the native tetramer. Journal of Biological Chemistry. ,vol. 269, pp. 4401- 4408 ,(1994) , 10.1016/S0021-9258(17)41794-7
R Brandsch, V Bichler, M Schmidt, J Buchner, GroE dependence of refolding and holoenzyme formation of 6-hydroxy-D-nicotine oxidase. Journal of Biological Chemistry. ,vol. 267, pp. 20844- 20849 ,(1992) , 10.1016/S0021-9258(19)36765-1
M Nagao, K Tanaka, FAD-dependent regulation of transcription, translation, post-translational processing, and post-processing stability of various mitochondrial acyl-CoA dehydrogenases and of electron transfer flavoprotein and the site of holoenzyme formation. Journal of Biological Chemistry. ,vol. 267, pp. 17925- 17932 ,(1992) , 10.1016/S0021-9258(19)37131-5
R. Brandsch, V. Bichler, Autoflavinylation of apo6-hydroxy-D-nicotine oxidase. Journal of Biological Chemistry. ,vol. 266, pp. 19056- 19062 ,(1991) , 10.1016/S0021-9258(18)55172-3
Maria Barile, Carmen Brizio, Daniela Valenti, Caterina De Virgilio, Salvatore Passarella, The riboflavin/FAD cycle in rat liver mitochondria FEBS Journal. ,vol. 267, pp. 4888- 4900 ,(2000) , 10.1046/J.1432-1327.2000.01552.X
Peter L. Pedersen, John W. Greenawalt, Baltazar Reynafarje, Joanne Hullihen, Glenn L. Decker, John W. Soper, Ernesto Bustamente, Preparation and characterization of mitochondria and submitochondrial particles of rat liver and liver-derived tissues. Methods in Cell Biology. ,vol. 20, pp. 411- 481 ,(1978) , 10.1016/S0091-679X(08)62030-0
Maria Barile, Carmen Brizio, Caterina Virgilio, Sebastiano Delfine, Ernesto Quagliariello, Salvatore Passarella, Flavin adenine dinucleotide and flavin mononucleotide metabolism in rat liver--the occurrence of FAD pyrophosphatase and FMN phosphohydrolase in isolated mitochondria. FEBS Journal. ,vol. 249, pp. 777- 785 ,(1997) , 10.1111/J.1432-1033.1997.00777.X
Silke Leimkühler, Werner Klipp, Role of XDHC in Molybdenum Cofactor Insertion into Xanthine Dehydrogenase of Rhodobacter capsulatus Journal of Bacteriology. ,vol. 181, pp. 2745- 2751 ,(1999) , 10.1128/JB.181.9.2745-2751.1999
Binhua P. Zhou, Duane A. Lewis, Sau-Wah Kwan, Creed W. Abell, Flavinylation of Monoamine Oxidase B Journal of Biological Chemistry. ,vol. 270, pp. 23653- 23660 ,(1995) , 10.1074/JBC.270.40.23653
TD Rae, PJ Schmidt, RA Pufahl, VC Culotta, T V. O'Halloran, Undetectable intracellular free copper: the requirement of a copper chaperone for superoxide dismutase. Science. ,vol. 284, pp. 805- 808 ,(1999) , 10.1126/SCIENCE.284.5415.805