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Titolo:
Functional diversity of LAP2 alpha and LAP2 beta in postmitotic chromosomeassociation is caused by an alpha-specific nuclear targeting domain
Autore:
Vlcek, S; Just, H; Dechat, T; Foisner, R;
Indirizzi:
Univ Vienna, Dept Biochem & Mol Cell Biol, Bioctr, A-1030 Vienna, Austria Univ Vienna Vienna Austria A-1030 l Biol, Bioctr, A-1030 Vienna, Austria
Titolo Testata:
EMBO JOURNAL
fascicolo: 22, volume: 18, anno: 1999,
pagine: 6370 - 6384
SICI:
0261-4189(19991115)18:22<6370:FDOLAA>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
ENVELOPE INNER MEMBRANE; LAMIN-B RECEPTOR; MATRIX ATTACHMENT REGIONS; CHROMATIN BINDING-SITE; NUCLEOCYTOPLASMIC TRANSPORT; DROSOPHILA-MELANOGASTER; INTEGRAL PROTEIN; ROD DOMAIN; DNA; POLYPEPTIDE-2;
Keywords:
chromosome; lamina-associated polypeptide; mitosis; nuclear lamina; nuclear matrix;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
46
Recensione:
Indirizzi per estratti:
Indirizzo: Foisner, R Univ Vienna, Dept Biochem & Mol Cell Biol, Bioctr, Dr Bohrgasse9, A-1030 Vienna, Austria Univ Vienna Dr Bohrgasse 9 Vienna Austria A-1030 enna, Austria
Citazione:
S. Vlcek et al., "Functional diversity of LAP2 alpha and LAP2 beta in postmitotic chromosomeassociation is caused by an alpha-specific nuclear targeting domain", EMBO J, 18(22), 1999, pp. 6370-6384

Abstract

Lamina-associated polypeptide 2 alpha (LAP2 alpha) is a non-membrane-boundisoform of the LAP2 family implicated in nuclear structure organization. We show that during postmitotic nuclear assembly LAP2 alpha associates with chromosomes prior to accumulation of the membrane-bound isoform LAP2 beta, 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 LAP2 alpha deletion mutants in HeLa cells, we identified an similar to 350-amino-acid-long region in the C-terminal alpha-specific domain of the protein that is required for retention of LAP2 alpha 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 LAP2 alpha mutants revealed that this LAP2 alpha-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.

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Documento generato il 29/03/20 alle ore 18:17:21