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P166 links membrane and intramitochondrial modules of the trypanosomal tripartite attachment complex

ABSTRACT: p166 is a central component of a protein complex that is essential for mitochondrial genome segregation in Trypanosoma brucei. The last 34 aa (the C-tail) of p166 are absolutely essential for its function of p166. The prupose of this experiment is to find even putative binding partners interacting with p166. For this purpose, two CoIP experiments with a truncated soluble version of p166 were performed. One uses p166 with an intact C-tail whereas the C-tail is removed in a second experiment. Differences between the two CoIPs indicate potential interactors of the C-tail.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Trypanosoma Brucei

TISSUE(S): Cell Culture

SUBMITTER: Julian Bender

LAB HEAD: Bettina Warscheid

PROVIDER: PXD033042 | Pride | 2022-06-02

REPOSITORIES: pride

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			Action	DRS
	20220330_mtHSP60-p166-HA.fasta	Fasta
	20220330_mtHSP60-p166-HA_short.fasta	Fasta
	QEplus033937.raw	Raw
	QEplus033939.raw	Raw
	QEplus033942.raw	Raw

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Publications

p166 links membrane and intramitochondrial modules of the trypanosomal tripartite attachment complex.

Schimanski Bernd B Aeschlimann Salome S Stettler Philip P Käser Sandro S Gomez-Fabra Gala Maria M Bender Julian J Warscheid Bettina B Vögtle F-Nora FN Schneider André A

PLoS pathogens 20220616 6

The protist parasite Trypanosoma brucei has a single mitochondrion with a single unit genome termed kinetoplast DNA (kDNA). Faithfull segregation of replicated kDNA is ensured by a complicated structure termed tripartite attachment complex (TAC). The TAC physically links the basal body of the flagellum with the kDNA spanning the two mitochondrial membranes. Here, we characterized p166 as the only known TAC subunit that is anchored in the inner membrane. Its C-terminal transmembrane domain separa ...[more]

PMID: 35709300

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