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Titolo:
THE ALPHA-HELICAL ROD DOMAIN OF HUMAN LAMIN-A AND LAMIN-C CONTAINS A CHROMATIN BINDING-SITE
Autore:
GLASS CA; GLASS JR; TANIURA H; HASEL KW; BLEVITT JM; GERACE L;
Indirizzi:
UNIV CALIF SAN DIEGO,SCRIPPS INST OCEANOG,RES INST,DEPT CELL BIOL,10666 N TORREY PINES RD LA JOLLA CA 92093 TELIOS PHARMACEUT SAN DIEGO CA 92121 PROGEN PHARMACEUT TARRYTOWN NY 10591 UNIV CALIF SAN DIEGO,SCRIPPS INST OCEANOG,RES INST,DEPT MOLEC BIOL LAJOLLA CA 92093
Titolo Testata:
EMBO journal
fascicolo: 11, volume: 12, anno: 1993,
pagine: 4413 - 4424
SICI:
0261-4189(1993)12:11<4413:TARDOH>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
INTERMEDIATE FILAMENT PROTEINS; NUCLEAR-PORE COMPLEX; PLASMA-MEMBRANE; INVITRO RECONSTITUTION; AVIAN ERYTHROCYTES; ESCHERICHIA-COLI; ENVELOPE; VIMENTIN; HEAD; ATTACHMENT;
Keywords:
CHROMATIN BINDING; LAMINS; ROD DOMAIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
39
Recensione:
Indirizzi per estratti:
Citazione:
C.A. Glass et al., "THE ALPHA-HELICAL ROD DOMAIN OF HUMAN LAMIN-A AND LAMIN-C CONTAINS A CHROMATIN BINDING-SITE", EMBO journal, 12(11), 1993, pp. 4413-4424

Abstract

We examined regions Of human lamins A and C involved in binding to surfaces of mitotic chromosomes. An Escherichia coli expression system was used to produce full-length lamin A and lamin C, and truncated lamins retaining the central alpha-helical rod domain (residues 34-388) but lacking various amounts of the amino-terminal 'head' and carboxy-terminal 'tail' domains. We found that lamin A, lamin C and lamin fragments lacking the head domain and tail sequences distal to residue 431 efficiently assembled into paracrystals and strongly associated with mitotic chromosomes. Furthermore, the lamin rod domain also associated with chromosomes, although efficient chromosome coating required the pH 5-6 conditions needed to assemble the rod into higher order structures. Biochemical assays showed that chromosomes substantially reduced thecritical concentration for assembly of lamin polypeptides into pelletable structures. Association of the lamin rod with chromosomes was abolished by pretrypsinization of chromosomes, and was not seen for vimentin (which possesses a similar rod domain). These data demonstrate that the alpha-helical rod of lamins A and C contains a specific chromosome binding site. Hence, the central rod domain of intermediate filament proteins can be involved in interactions with other cellular structures as well as in filament assembly.

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Documento generato il 03/06/20 alle ore 09:36:32