Solubility properties and specific assembly pathways of the B-type lamin from Caenorhabditis elegans

Nicole Foeger, Naama Wiesel, Dorothee Lotsch, Norbert Mücke, Laurent Kreplak, Ueli Aebi, Yosef Gruenbaum, Harald Herrmann

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52 Citas (Scopus)

Resumen

Lamins are nucleus-specific intermediate filament (IF) proteins that together with a complex set of membrane proteins form a filamentous meshwork tightly adhering to the inner nuclear membrane and being associated with the nuclear pore complexes. This so-called nuclear lamina provides mechanical stability and, in addition, has been implicated in the spatial organization of the heterochromatin. While increasing knowledge on the biological function of lamins has been obtained in recent years, the assembly mechanism of lamin filaments at the molecular level has remained largely elusive. Therefore, we have now more systematically investigated lamin assembly in vitro. Using Caenorhabditis elegans lamin, which has been reported to assemble into 10-nm filaments under low ionic strength conditions, we investigated the assembly kinetics of this protein into filaments in more detail using both His-tagged and un-tagged recombinant proteins. In particular, we have characterized distinct intermediates in the filament assembly process by analytical ultracentrifugation, electron and atomic force microscopy. In contrast to the general view that lamins assemble only slowly into filaments, we show that in vitro association reactions are extremely fast, and depending on the ionic conditions employed, significant filamentous assemblies form within seconds.

Idioma originalEnglish
Páginas (desde-hasta)340-350
Número de páginas11
PublicaciónJournal of Structural Biology
Volumen155
N.º2
DOI
EstadoPublished - ago. 2006
Publicado de forma externa

Nota bibliográfica

Funding Information:
N.F. was a recipient of an E. Schroedinger Postdoc fellowship of the Austrian Science Fund (FWF). Y.G. and H.H. were supported the Cooperation Program in Cancer Research of the Deutsches Krebsforschungszentrum (DKFZ) and Israel’s Ministry of Science and Technology (MOST) Grant CA107. U.A.’s research was supported by a grant from the Swiss National Science Foundation, by a National Center of Competence in Research (NCCR) on “Nanoscale Science,” the M.E. Müller Foundation of Switzerland, and the Canton Basel-Stadt.

ASJC Scopus Subject Areas

  • Structural Biology

PubMed: MeSH publication types

  • Journal Article
  • Research Support, Non-U.S. Gov't

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