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A hub-and-spoke nuclear amina architecture in trypanosomes
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SYSNO ASEP 0554434 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title A hub-and-spoke nuclear amina architecture in trypanosomes Author(s) Padilla-Mejia, N.E. (GB)
Kořený, L. (CZ)
Holden, J. (GB)
Vancová, Marie (BC-A) RID, ORCID
Lukeš, Julius (BC-A) RID, ORCID
Zoltner, M. (CZ)
Field, Mark Christian (BC-A) ORCIDNumber of authors 7 Article number jcs251264 Source Title Journal of Cell Science. - : Company of Biologists - ISSN 0021-9533
Roč. 134, č. 12 (2021)Number of pages 16 s. Publication form Online - E Language eng - English Country GB - United Kingdom 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 Subject RIV EB - Genetics ; Molecular Biology OECD category Genetics and heredity (medical genetics to be 3) R&D Projects EF16_019/0000759 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) LM2015062 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) Method of publishing Open access Institutional support BC-A - RVO:60077344 UT WOS 000679477200003 EID SCOPUS 85108765882 DOI 10.1242/jcs.251264 Annotation 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. Workplace Biology Centre (since 2006) Contact Dana Hypšová, eje@eje.cz, Tel.: 387 775 214 Year of Publishing 2022 Electronic address https://journals.biologists.com/jcs/article/134/12/jcs251264/269176/A-hub-and-spoke-nuclear-lamina-architecture-in
Number of the records: 1