A hub and spoke nuclear lamina architecture in trypanosomes

Norma Padilla-Mejia, Ludek Koreny, Jennifer Holden, Marie Vancová, Julius Lukeš, Martin Zoltner, Mark C. Field (Lead / Corresponding author)

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Abstract

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 the ∼60 kDa lamin-based system of metazoa and other lineages. To uncover organizational principles for the trypanosome laminawe 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- 1 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.

Original languageEnglish
Article numberjcs251264
Number of pages16
JournalJournal of Cell Science
Volume134
Issue number12
Early online date19 May 2021
DOIs
Publication statusPublished - 21 Jun 2021

Keywords

  • lamina
  • macromolecular assembly
  • trypanosomatids
  • nuclear organisation
  • heterochromatin
  • Heterochromatin
  • Trypanosomatid
  • Nuclear organization
  • Macromolecular assembly
  • Lamina

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