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Proteomic analysis of mitoUFD binding partners

ABSTRACT: This project is to identify the binding partners of the OMM anchored ubiquitin-fusion degradation substrate (mitoUFD) in comparison with the mitoGFP control that lacks the ubiquitin fusion as the degradation signal. In addition, we performed RNAi knockdown for bcat-1, lars-1 and gcn-2 compared to the L4440 RNAi control to identify the changes of mitoUFD binding partners upon disruption of leucine catabolism or sensing.

INSTRUMENT(S):

ORGANISM(S): Caenorhabditis Elegans

TISSUE(S): Whole Body

SUBMITTER: Prerana Wagle

LAB HEAD: Thorsten Hoppe

PROVIDER: PXD062734 | Pride | 2025-11-05

REPOSITORIES: Pride

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			Action	DRS
	E3_3952_01.raw	Raw
	E3_3952_02.raw	Raw
	Experiment.txt	Txt
	PRIDE_3952.zip	Other
	PRIDE_4015.zip	Other

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Role of TbTim20 in mitochondrial protein import in trypanosomes – TbTim20 RNAi data

Project description:Protein import across the mitochondrial inner membrane typically depends on two protein translocases of the inner membrane (TIM) complexes and the membrane potential. The protozoan parasite Trypanosoma brucei, however, has a single, divergent TIM complex. Unlike other trypanosomal TIM subunits, TbTim20 is neither essential for normal growth of insect nor bloodstream forms of T. brucei, leaving its role uncertain. Specific mutations in the γ-subunit of the F1FO-ATPase, such as γL262P, permit bloodstream form trypanosomes to grow without mitochondrial DNA (kinetoplast or kDNA). Here we show that RNAi-mediated depletion of TbTim20 inhibits growth of this cell line, but only if it lacks the kDNA. Titration of mitochondrial uncouplers and direct membrane potential measurements reveal that TbTim20 becomes more critical as the membrane potential decreases across all tested lines. Proteomic analysis of the uninduced and induced γL262P TbTim20-RNAi cell line, which lacks kDNA and exhibits the lowest membrane potential, shows depletion of a subset of imported proteins. This subset includes ATPase subunits, explaining why TbTim20-silenced cell lines become more sensitive to uncouplers. Thus, we propose that TbTim20 supports import of a subset of proteins whose import is hypersensitive to a low membrane potential.

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Proteomic analysis of leucine effect on OMM protein turnover in C. elegans overexpressing cdc-48

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The Caenorhabditis elegans RDE-10/RDE-11 complex regulates RNAi by promoting secondary siRNA amplification

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