PXD019978 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Effect of truncation mutants of the trypanosomatid nuclear lamina protein NUP-1 on the whole cell proteome in T. brucei |
Description | The nuclear lamina has multiple functions, including maintaining nuclear structural integrity and differential gene expression. Correct spatial and temporal lamina assembly is essential to meet these and other roles. Recently, it emerged that multiple lamina systems exist that are likely products of independent origins, while all these systems share remarkably analogous functions. Several lamina proteins are known in trypanosomes, two of which, NUP-1 and NUP-2, are essential, coiled-coil proteins with a molecular mass 450 and 250 kDa, respectively. Sequence analysis indicates distinct quaternary structures when compared to the ~60 kDa lamin proteins of multiple lineages, including metazoa. To uncover organisational principles of the trypanosome lamina we generated NUP-1 deletion mutants (N=N-terminal domain; C= C-terminal domain; NC: fusion of the N- and C-terminal domain with entire repeat region deletedd))designed to identify domains of NUP-1 responsible for oligomerisation. We find that both N- and C-termini act as interaction domains and disruption of these interactions impacts additional components of the lamina, the nuclear envelope and nucleoporin TbNup98. By contrast there is remarkably little impact on transcription, crucially including silencing of telomeric variant surface glycoprotein genes. These data indicate that both terminal domains of NUP-1 have roles in assembling the trypanosome lamina and suggest an architecture distinct to the lamin system is based on a ‘hub and spoke’ configuration. |
HostingRepository | PRIDE |
AnnounceDate | 2024-10-22 |
AnnouncementXML | Submission_2024-10-22_05:22:35.375.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Martin Zoltner |
SpeciesList | scientific name: Trypanosoma brucei brucei TREU927; NCBI TaxID: 185431; |
ModificationList | monohydroxylated residue; acetylated residue |
Instrument | Q Exactive |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2020-06-23 18:15:20 | ID requested | |
1 | 2021-06-03 08:12:46 | announced | |
⏵ 2 | 2024-10-22 05:22:35 | announced | 2024-10-22: Updated project metadata. |
Publication List
Dataset with its publication pending |
Keyword List
submitter keyword: lamina, trypanosoma, nuclear organisation, molecular assembly, heterochromatin |
Contact List
Mark C. Field |
contact affiliation | Mark C. Field Professor of Cell Biology and Parasitology Division of Biological Chemistry & Drug Discovery School of Life Sciences University of Dundee Dundee United Kingdom |
contact email | mfield@mac.com |
lab head | |
Martin Zoltner |
contact affiliation | Division of Biological Chemistry & Drug Discovery School of Life Sciences University of Dundee Dundee DD1 5EH |
contact email | m.zoltner@dundee.ac.uk |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD019978
- Label: PRIDE project
- Name: Effect of truncation mutants of the trypanosomatid nuclear lamina protein NUP-1 on the whole cell proteome in T. brucei