DNA cross-link repair protein SNM1A interacts with PIAS1 in nuclear focus formation.
Mol Cell Biol
; 24(24): 10733-41, 2004 Dec.
Article
em En
| MEDLINE
| ID: mdl-15572677
ABSTRACT
The yeast SNM1/PSO2 gene specifically functions in DNA interstrand cross-link (ICL) repair, and its role has been suggested to be separate from other DNA repair pathways. In vertebrates, there are three homologs of SNM1 (SNM1A, SNM1B, and SNM1C/Artemis; SNM1 family proteins) whose functions are largely unknown. We disrupted each of the SNM1 family genes in the chicken B-cell line DT40. Both SNM1A- and SNM1B-deficient cells were sensitive to cisplatin but not to X-rays, whereas SNM1C/Artemis-deficient cells exhibited sensitivity to X-rays but not to cisplatin. SNM1A was nonepistatic with XRCC3 (homologous recombination), RAD18 (translesion synthesis), FANCC (Fanconi anemia), and SNM1B in ICL repair. SNM1A protein formed punctate nuclear foci depending on the conserved SNM1 (metallo-beta-lactamase) domain. PIAS1 was found to physically interact with SNM1A, and they colocalized at nuclear foci. Point mutations in the SNM1 domain, which disrupted the interaction with PIAS1, led to mislocalization of SNM1A in the nucleus and loss of complementation of snm1a cells. These results suggest that interaction between SNM1A and PIAS1 is required for ICL repair.
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1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
DNA Fúngico
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Proteínas Fúngicas
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Proteínas Nucleares
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Proteínas de Saccharomyces cerevisiae
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Proteínas Modificadoras Pequenas Relacionadas à Ubiquitina
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Proteínas de Ligação a DNA
Idioma:
En
Ano de publicação:
2004
Tipo de documento:
Article