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Regulation of respiratory complex I assembly by FMN cofactor targeting

ABSTRACT: Regulation of respiratory complex I assembly by FMN cofactor targeting

PROVIDER: PRJNA1047500 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR27010871.fastq.gz	Fastqsanger.gz
	SRR27010872.fastq.gz	Fastqsanger.gz
	SRR27010873.fastq.gz	Fastqsanger.gz
	SRR27010874.fastq.gz	Fastqsanger.gz
	SRR27010875.fastq.gz	Fastqsanger.gz

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Regulation of respiratory complex I assembly by FMN cofactor targeting

Project description:The main objective of this study is to answer whether the stability of mammalian complex I is regulated by its flavin cofactor. For this purpose, diphenyleneiodonium (DPI) was used as inhibitor of N-module, to evaluate stability in in CI

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Assembly of respiratory complex I is regulated by FMN insertion into the N-module.

Project description:Respiratory complex I plays a crucial role in the mitochondrial electron transport chain and shows promise as a therapeutic target for various human diseases. While most studies focus on inhibiting complex I at the Q-site, little is known about inhibitors targeting other sites within the complex. In this study, we demonstrate that diphenyleneiodonium (DPI), a known N-site inhibitor, uniquely affects the stability of complex I by inhibiting its flavin cofactor FMN. Treatment with DPI blocks the final stage of complex I assembly, leading to the accumulation of assembly intermediates that lack the N-module. Remarkably, high-dose DPI treatment can completely and reversibly degrade complex I in different cellular models. The mechanism involves the accumulation of DPI in mitochondria, where it reacts with FMN, depleting the effective pool of FMN and halting complex I maturation. Consistently, growing cells in medium lacking the FMN precursor riboflavin or knocking out the mitochondrial FAD carrier gene SLC25A32 results in complex I degradation and impairs complex I-dependent respiration. Overall, our findings establish a direct connection between mitochondrial flavin homeostasis and complex I stability and assembly, paving the way for novel pharmacological strategies to regulate respiratory complex I.

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Project description:The Mitochondrial Complex I Assembly (MCIA) complex is essential for the biogenesis of respiratory Complex I (CI), the first enzyme in the respiratory chain, which has been linked to Alzheimer’s disease (AD) pathogenesis. However, how MCIA facilitates CI assembly, and how it is linked with AD pathogenesis, is poorly understood. Here we report the structural basis of the complex formation between the MCIA subunits ECSIT and ACAD9. ECSIT binding induces a major conformational change in the FAD-binding loop of ACAD9, releasing the FAD cofactor and converting ACAD9 from a fatty acid β-oxidation (FAO) enzyme to a CI assembly factor. We provide evidence that ECSIT phosphorylation downregulates its association with ACAD9 and is reduced in neuronal cells upon exposure to amyloid-β (Aβ) oligomers. These findings advance our understanding of the MCIA complex assembly and suggest a possible role for ECSIT in the reprogramming of bioenergetic pathways linked to Aβ toxicity, a hallmark of AD.

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Fidelity of translation initiation is required for coordinated respiratory complex assembly

Project description:Mammalian mitochondrial ribosomes are unique molecular machines that translate 11 leaderless mRNAs. To date it is not clear how mitoribosomes recognize and initiate translation in the absence of untranslated regions in the mitochondrial mRNAs. Translation initiation in mitochondria shares similarities with prokaryotic systems, such as the formation of a ternary complex of fMet-tRNAMet, mRNA and the 28S subunit, but differs in the requirements for initiation factors. Mitochondria have two initiation factors, MTIF2 that closes the decoding centre and stabilizes the binding of the fMet-tRNAMet to the leaderless mRNAs, and MTIF3 whose role is not clear. We knocked out Mtif3 in mice and show that this protein is essential for embryo development and heart- and skeletal muscle-specific loss of MTIF3 causes premature death. We identify increased but uncoordinated mitochondrial protein synthesis in mice lacking MTIF3 that results in loss of specific respiratory complexes. Therefore, we show that coordinated assembly of OXPHOS complexes requires stoichiometric levels of nuclear and mitochondrially-encoded protein subunits in vivo. Our ribosome profiling and transcriptomic analyses show that MTIF3 is required for recognition and regulation of translation initiation of mitochondrial mRNAs, but not dissociation of the ribosome subunits.

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