Saijo T, Tanaka K
Department of Genetics, Yale University School of Medicine, New Haven, Connecticut 06510.
J Biol Chem. 1995 Jan 27;270(4):1899-907. doi: 10.1074/jbc.270.4.1899.
We studied the role of FAD in the intramitochondrial folding and assembly of medium-chain acyl-CoA dehydrogenase (MCAD), a homotetrameric mitochondrial enzyme containing a molecule of non-covalently bound FAD/monomer. In the MCAD molecule, FAD is buried in a crevice containing the active center. We have previously shown that upon import into mitochondria, newly processed MCAD is first incorporated into a high molecular weight (hMr) complex and that the hMr complex mainly consisted of MCAD-heat-shock protein 60 (hsp60) complex (Saijo, T., Welch, W.J., and Tanaka, K (1994) J. Biol. Chem. 269, 4401-4408). In the present study, we incubated in vitro synthesized precursor MCAD with mitochondria isolated from normal and riboflavin-deficient rat liver for 10-60 min and fractionated the solubilized mitochondria using gel filtration. The amount of MCAD in the hMr complex was larger and that of tetramer was smaller in riboflavin-deficient mitochondria than in control at any time point. In addition, riboflavin-deficient mitochondria were solubilized after 10-min import in a buffer containing ATP and were chased in the presence of FAD, FMN, or NAD+ or without any addition. The mitochondrial proteins were analyzed using gel filtration or immunoprecipitated with anti-hsp60 antibody. After 60-min chase in the presence of FAD, the majority of MCAD in the complex with hsp60 was transferred to tetramer, whereas no such transfer occurred after the chase in the absence of FAD. When chase was done in the presence of FMN, a significant amount of MCAD was transferred from the complex with hsp60 to tetramer, but the transfer was not as efficient as in the presence of FAD. The chase in the presence of NAD+ resulted in no transfer. These data suggest that isoalloxazine ring of FAD plays a critical role, exerting nucleating effect, in the hsp60-assisted folding of MCAD subunit into an assembly competent conformation, probably assisting the formation of the core.
我们研究了黄素腺嘌呤二核苷酸(FAD)在中链酰基辅酶A脱氢酶(MCAD)线粒体内折叠和组装过程中的作用,MCAD是一种同四聚体线粒体酶,每个单体含有一个非共价结合的FAD分子。在MCAD分子中,FAD埋藏在含有活性中心的裂隙中。我们之前已经表明,新加工的MCAD导入线粒体后,首先会整合到一个高分子量(hMr)复合物中,并且该hMr复合物主要由MCAD-热休克蛋白60(hsp60)复合物组成(斋藤,T.,韦尔奇,W.J.,和田中,K(1994)《生物化学杂志》269,4401-4408)。在本研究中,我们将体外合成的前体MCAD与从正常和核黄素缺乏的大鼠肝脏分离的线粒体一起孵育10 - 60分钟,然后使用凝胶过滤对溶解的线粒体进行分级分离。在任何时间点,核黄素缺乏的线粒体中hMr复合物中的MCAD量都比对照中的大,而四聚体的量则比对照中的小。此外,核黄素缺乏的线粒体在含有ATP的缓冲液中导入10分钟后进行溶解,并在FAD、黄素单核苷酸(FMN)或烟酰胺腺嘌呤二核苷酸(NAD +)存在或无任何添加物的情况下进行追踪。使用凝胶过滤分析线粒体蛋白,或用抗hsp60抗体进行免疫沉淀。在FAD存在下追踪60分钟后,与hsp60结合的复合物中的大多数MCAD转移到了四聚体中,而在没有FAD的情况下追踪后则没有发生这种转移。当在FMN存在下进行追踪时,大量的MCAD从与hsp60的复合物转移到了四聚体中,但转移效率不如在FAD存在时高。在NAD +存在下进行追踪没有导致转移。这些数据表明,FAD的异咯嗪环在hsp60辅助MCAD亚基折叠成可组装构象的过程中起着关键作用,发挥成核效应,可能有助于核心的形成。