| Registro completo |
| Provedor de dados: |
ArchiMer
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| País: |
France
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| Título: |
Structure and function of a novel endonuclease acting on branched DNA substrates
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| Autores: |
Ren, Bin
Kuehn, Joelle
Meslet-cladiere, Laurence
Briffotaux, Julien
Norais, Cedric
Lavigne, Regis
Flament, Didier
Ladenstein, Rudolf
Myllykallio, Hannu
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| Data: |
2009-08
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| Ano: |
2009
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| Palavras-chave: |
Structure function studies
RecB family
Novel endonuclease
DNA repair
Branched DNA structures
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| Resumo: |
We show that Pyrococcus abyssi PAB2263 (dubbed NucS (nuclease for ss DNA) is a novel archaeal endonuclease that interacts with the replication clamp PCNA. Structural determination of P. abyssi NucS revealed a two-domain dumbbell-like structure that in overall does not resemble any known protein structure. Biochemical and structural studies indicate that NucS orthologues use a non-catalytic ssDNA-binding domain to regulate the cleavage activity at another site, thus resulting into the specific cleavage at double-stranded DNA (dsDNA)/ssDNA junctions on branched DNA substrates. Both 3' and 5' extremities of the ssDNA can be cleaved at the nuclease channel that is too narrow to accommodate duplex DNA. Altogether, our data suggest that NucS proteins constitute a new family of structure-specific DNA endonucleases that are widely distributed in archaea and in bacteria, including Mycobacterium tuberculosis.
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| Tipo: |
Text
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| Idioma: |
Inglês
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| Identificador: |
http://archimer.ifremer.fr/doc/2009/publication-6807.pdf
DOI:10.1038/emboj.2009.192
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| Editor: |
Nature Publishing Group
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| Relação: |
http://archimer.ifremer.fr/doc/00000/6807/
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| Formato: |
application/pdf
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| Fonte: |
Embo Journal (0261-4189) (Nature Publishing Group), 2009-08 , Vol. 28 , N. 16 , P. 2479-2489
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| Direitos: |
2009 European Molecular Biology Organization ; Nature
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