ND3, ND1 and 39 kDa subunits are more exposed in the de-active form of bovine mitochondrial complex I

被引:38
作者
Babot, Marion [1 ]
Labarbuta, Paola [1 ]
Birch, Amanda [1 ]
Kee, Sara [1 ]
Fuszard, Matthew [2 ]
Botting, Catherine H. [2 ]
Wittig, Ilka [3 ]
Heide, Heinrich [3 ]
Galkin, Alexander [1 ]
机构
[1] Queens Univ Belfast, Sch Biol Sci, Ctr Med Biol, Belfast BT9 7BL, Antrim, North Ireland
[2] Univ St Andrews, Sch Chem, BMS Annexe, St Andrews KY16 9ST, Fife, Scotland
[3] Goethe Univ Frankfurt, Fac Med, SFB Core Unit, D-60590 Frankfurt, Germany
来源
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS | 2014年 / 1837卷 / 06期
关键词
Complex I; NADH:ubiquinone oxidoreductase; A/D transition; Conformational change; Protein tyrosine modification; N-hydroxysuccinimide; NADH-UBIQUINONE OXIDOREDUCTASE; CLEAR-NATIVE ELECTROPHORESIS; ESCHERICHIA-COLI NDH-1; CHEMICAL CROSS-LINKING; INACTIVE TRANSITION; MEMBRANE DOMAIN; CONFORMATIONAL-CHANGE; HEART-MITOCHONDRIA; RESPIRATORY-CHAIN; MASS-SPECTROMETRY;
D O I
10.1016/j.bbabio.2014.02.013
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
An intriguing feature of mitochondrial complex I from several species is the so-called A/D transition, whereby the idle enzyme spontaneously converts from the active (A) form to the de-active (D) form. The A/D transition plays an important role in tissue response to the lack of oxygen and hypoxic deactivation of the enzyme is one of the key regulatory events that occur in mitochondria during ischaemia. We demonstrate for the first time that the A/D conformational change of complex I does not affect the macromolecular organisation of supercomplexes in vitro as revealed by two types of native electrophoresis. Cysteine 39 of the mitochondrially-encoded ND3 subunit is known to become exposed upon de-activation. Here we show that even if complex I is a constituent of the I + III2 + IV (S-1) supercomplex, cysteine 39 is accessible for chemical modification in only the D-form. Using lysine-specific fluorescent labelling and a DICE-like approach we further identified two new subunits involved in structural rearrangements during the A/D transition: ND1 (MT-ND1) and 39 kDa (NDUFA9). These results clearly show that structural rearrangements during de-activation of complex I include several subunits located at the junction between hydrophilic and hydrophobic domains, in the region of the quinone binding site. De-activation of mitochondrial complex I results in concerted structural rearrangement of membrane subunits which leads to the disruption of the sealed quinone chamber required for catalytic turnover. Crown Copyright (C) 2014 Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:929 / 939
页数:11
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