Premium
Functional diversity of LAP2α and LAP2β in postmitotic chromosome association is caused by an α‐specific nuclear targeting domain
Author(s) -
Vlcek Sylvia,
Just Herwig,
Dechat Thomas,
Foisner Roland
Publication year - 1999
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/18.22.6370
Subject(s) - biology , genetics , chromosome , microbiology and biotechnology , association (psychology) , computational biology , gene , philosophy , epistemology
Lamina‐associated polypeptide 2α (LAP2α) is a non‐membrane‐bound isoform of the LAP2 family implicated in nuclear structure organization. We show that during postmitotic nuclear assembly LAP2α associates with chromosomes prior to accumulation of the membrane‐bound isoform LAP2β, although both proteins contain the same putative chromatin interaction domains located in their common N‐terminal regions. By transient and stable expression of various N‐ and C‐terminal LAP2α deletion mutants in HeLa cells, we identified an ∼350‐amino‐acid‐long region in the C‐terminal α‐specific domain of the protein that is required for retention of LAP2α in interphase nuclei and for association with mitotic chromosomes, while the N‐terminal domain seemed to be dispensable for these interactions. In vitro chromosome binding studies using recombinant LAP2α mutants revealed that this LAP2α‐specific ‘nuclear targeting domain’ was essential and sufficient for association with chromosomes. These data suggested a functional diversity of chromosome binding properties of LAP2 isoforms.