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心磷脂酰基链组成对线粒体复合物稳定性的影响;心磷脂在α-酮戊二酸脱氢酶和阻遏蛋白复合物中的意想不到的作用。

The influence of the acyl chain composition of cardiolipin on the stability of mitochondrial complexes; an unexpected effect of cardiolipin in alpha-ketoglutarate dehydrogenase and prohibitin complexes.

机构信息

Biomolecular Mass Spectrometry and Proteomics Group, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands.

出版信息

J Proteomics. 2010 Feb 10;73(4):806-14. doi: 10.1016/j.jprot.2009.11.009. Epub 2009 Nov 24.

Abstract

The role of cardiolipin acyl chain composition in assembly/stabilization of mitochondrial complexes was investigated using three yeast deletion mutants (acb1Delta strain; taz1Delta strain; and acb1Deltataz1Delta strain). Deletion of the TAZ1 gene, involved in cardiolipin acyl chain remodeling, is known to increase the content of monolyso-cardiolipin (MLCL) at the expense of CL, and to decrease the unsaturation of the remaining CL. Deletion of the ACB1 gene encoding the acyl-CoA-binding protein, involved in fatty acid elongation, decreases the average length of the CL acyl chains. Furthermore, a TAZ1ACB1 double deletion mutant strain was used in this study which has both a decrease in the length of the CL acyl chains and an increase in MLCL. BN/SDS PAGE analysis revealed that cardiolipin is important for the prohibitin-m-AAA protease complex, the alpha-ketoglutarate dehydrogenase complex and respiratory chain supercomplexes. The results indicate that the decreased level of complexes in taz1Delta and acb1Deltataz1Delta mitochondria is due to a decreased content of CL or the presence of MLCL.

摘要

使用三种酵母缺失突变体(acb1Δ 株;taz1Δ 株;acb1Δtaz1Δ 株)研究了心磷脂酰基链组成在线粒体复合物的组装/稳定中的作用。TAZ1 基因的缺失涉及心磷脂酰基链重塑,已知会增加单酰基心磷脂(MLCL)的含量,而降低剩余 CL 的不饱和程度。编码酰基辅酶 A 结合蛋白的 ACB1 基因的缺失,参与脂肪酸延长,降低了 CL 酰基链的平均长度。此外,在这项研究中使用了 TAZ1ACB1 双缺失突变体菌株,其 CL 酰基链长度降低,MLCL 增加。BN/SDS PAGE 分析表明心磷脂对于抑制素-m-AAA 蛋白酶复合物、α-酮戊二酸脱氢酶复合物和呼吸链超复合物很重要。结果表明,taz1Δ 和 acb1Δtaz1Δ 线粒体中复合物水平的降低是由于 CL 含量降低或存在 MLCL 所致。

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