PXD062506 is an
original dataset announced via ProteomeXchange.
Dataset Summary
| Title | Beyond a linear structure: The Tubular of the Tripartite Attachment Complex and the Functional Role of TAC53 |
| Description | The tripartite attachment complex (TAC) is essential for mitochondrial DNA (kDNA) segregation in Trypanosoma brucei, providing a physical link between the flagellar basal body and the mitochondrial genome. Although the TAC's hierarchical assembly and linear organization have been extensively studied, much remains to be discovered regarding its complete architecture and composition – for instance, our identification of a new TAC component underscores these knowledge gaps. Here, we use a combination of proteomics, RNA interference (RNAi), and Ultrastructure Expansion Microscopy (U-ExM) to characterize the TAC at high resolution and identify a novel component, TAC53 (Tb927.2.6100). Depletion of TAC53 in both procyclic and bloodstream forms results in kDNA missegregation and loss, a characteristic feature of TAC dysfunction. TAC53 localizes to the kDNA in a cell cycle–dependent manner and represents the most kDNA-proximal TAC component identified to date. U-ExM reveals a previously unrecognized tubular architecture of the TAC, with two distinct TAC structures per kDNA disc, suggesting a mechanism for precise kDNA alignment and segregation. Moreover, immunoprecipitation and imaging analyses indicate that TAC53 interacts with known TAC-associated proteins HMG44, KAP68, and KAP3, forming a network at the TAC-kDNA interface. These findings redefine our understanding of TAC architecture and function and identify TAC53 as a key structural component anchoring the mitochondrial genome in T. brucei. |
| HostingRepository | PRIDE |
| AnnounceDate | 2025-08-11 |
| AnnouncementXML | Submission_2025-08-11_03:08:21.489.xml |
| DigitalObjectIdentifier | |
| ReviewLevel | Peer-reviewed dataset |
| DatasetOrigin | Original dataset |
| RepositorySupport | Unsupported dataset by repository |
| PrimarySubmitter | Manfred Heller |
| SpeciesList | scientific name: Trypanosoma brucei; NCBI TaxID: 5691; |
| ModificationList | monohydroxylated residue; acetylated residue; iodoacetamide derivatized residue |
| Instrument | Orbitrap Fusion Lumos; Q Exactive HF |
Dataset History
| Revision | Datetime | Status | ChangeLog Entry |
| 0 | 2025-04-02 01:48:58 | ID requested | |
| ⏵ 1 | 2025-08-11 03:08:21 | announced | |
Publication List
| Dataset with its publication pending |
Keyword List
| submitter keyword: Tripartite Attachment Complex, Expansion Microscopy,Trypanosoma brucei |
Contact List
| Torsten Ochsenreiter |
| contact affiliation | Institute of Cell Biology, University of Bern, 3012 Bern, Switzerland |
| contact email | torsten.ochsenreiter@unibe.ch |
| lab head | |
| Manfred Heller |
| contact affiliation | Proteomics and Mass Spectrometry Core Facility,
Departement for Biomedical Research,
University of Berne |
| contact email | pmscf.dbmr@unibe.ch |
| dataset submitter | |
Full Dataset Link List
Dataset FTP location
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| PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD062506
- Label: PRIDE project
- Name: Beyond a linear structure: The Tubular of the Tripartite Attachment Complex and the Functional Role of TAC53