A hub-and-spoke nuclear amina architecture in trypanosomes

0554434 - BC 2022 RIV GB eng J - Journal Article
Padilla-Mejia, N.E. - Kořený, L. - Holden, J. - Vancová, Marie - Lukeš, Julius - Zoltner, M. - Field, Mark Christian
A hub-and-spoke nuclear amina architecture in trypanosomes.
Journal of Cell Science. Roč. 134, č. 12 (2021), č. článku jcs251264. ISSN 0021-9533. E-ISSN 1477-9137
R&D Projects: GA MŠMT(CZ) EF16_019/0000759; GA MŠMT(CZ) LM2015062
EU Projects: Wellcome Trust(GB) 204697/Z/16/Z
Institutional support: RVO:60077344
Keywords : lamin-a/c expression * blood-stream forms * pore complex * functional-characterization * structural organization * envelope alterations * antigenic variation * gene-expression * cell-cycle * a-type * Lamina * Macromolecular assembly * Trypanosomatid * Nuclear organization * Heterochromatin
OECD category: Genetics and heredity (medical genetics to be 3)
Impact factor: 5.235, year: 2021
Method of publishing: Open access
https://journals.biologists.com/jcs/article/134/12/jcs251264/269176/A-hub-and-spoke-nuclear-lamina-architecture-in

The nuclear lamina supports many functions, including maintaining nuclear structure and gene expression control, and correct spatiotemporal assembly is vital to meet these activities. Recently, multiple lamina systems have been described that, despite independent evolutionary origins, share analogous functions. In trypanosomatids the two known lamina proteins, NUP-1 and NUP-2, have molecular masses of 450 and 170 kDa, respectively, which demands a distinct architecture from the60 kDa lamin-based system of metazoa and other lineages. To uncover organizational principles for the trypanosome lamina we generated NUP-1 deletion mutants to identify domains and their arrangements responsible for oligomerization. We found that both the N- and C-termini act as interaction hubs, and that perturbation of these interactions impacts additional components of the lamina and nuclear envelope. Furthermore, the assembly of NUP-I terminal domains suggests intrinsic organizational capacity. Remarkably, there is little impact on silencing of telomeric variant surface glycoprotein genes. We suggest that both terminal domains of NUP-1 have roles in assembling the trypanosome lamina and propose a novel architecture based on a hub-and-spoke configuration.
Permanent Link: http://hdl.handle.net/11104/0329144