Proteomics

Dataset Information

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Probing the trypanosome nuclear pore by TurboID proximity labelling

ABSTRACT: Previous BioID experiments targeting the nucleoporin (NUP) NUP158 and the nuclear transport factor MEX67 indicated (PMID: 36410438; PXD031245) that proximity labelling delivers highly specific interactome data in the confined localisation of the nuclear pore, with a labelling radius well below the size of the nuclear pore. Here we extended this approach to target NUPs NUP110, NUP76 and NUP96 with a TurboID-HA tandem tag fused to both, the N and C-terminus of each respective target protein. While the central NUP96 biotinylated most nuclear pore proteins with the marked exception of the nuclear basket, NUP158, NUP110 and NUP76 caused biotinylation of specific sub-complexes of the pore and Mex67 labelled NUPs lining the pore channel.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Trypanosoma Brucei

TISSUE(S): Permanent Cell Line Cell

DISEASE(S): Trypanosomiasis

SUBMITTER: Martin Zoltner  

LAB HEAD: Dr. Martin Zoltner

PROVIDER: PXD047268 | Pride | 2023-12-04

REPOSITORIES: Pride

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Dataset's files

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Action DRS
BioID_PCF_NUP110NUP76NUP96_output.txt.rar Txt
NUP110C_1.raw Raw
NUP110C_2.raw Raw
NUP110N_1.raw Raw
NUP110N_2.raw Raw
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Publications

Impact of inherent biases built into proteomic techniques: Proximity labeling and affinity capture compared.

Moreira Claudia Maria do Nascimento CMDN   Kelemen Cristina D CD   Obado Samson O SO   Zahedifard Farnaz F   Zhang Ning N   Holetz Fabiola B FB   Gauglitz Laura L   Dallagiovanna Bruno B   Field Mark C MC   Kramer Susanne S   Zoltner Martin M  

The Journal of biological chemistry 20221119 1

The characterization of protein-protein interactions (PPIs) is of high value for understanding protein function. Two strategies are popular for identification of PPIs direct from the cellular environment: affinity capture (pulldown) isolates the protein of interest with an immobilized matrix that specifically captures the target and potential partners, whereas in BioID, genetic fusion of biotin ligase facilitates proximity biotinylation, and labeled proteins are isolated with streptavidin. Whils  ...[more]

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