Data/hora: 16/06/2024 17:10:32

Provedor de dados: 	Institutional Archive of Ifreme (ArchiMer)	
País: 	France	
Título: 	Structure and function of a novel endonuclease acting on branched DNA substrates	
Autores: 	Ren, Bin; Kuehn, Joelle; Meslet-cladiere, Laurence; Briffotaux, Julien; Norais, Cedric; Lavigne, Regis; Flament, Didier; Ladenstein, Rudolf; Myllykallio, Hannu.	
Data: 	2009-08	
Ano: 	2009	
Palavras-chave: 	Structure function studies; RecB family; Novel endonuclease; DNA repair; Branched DNA structures.	
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.	
Tipo: 	Text	
Idioma: 	Inglês	
Identificador: 	http://archimer.ifremer.fr/doc/2009/publication-6807.pdf

DOI:10.1038/emboj.2009.192	
Editor: 	Nature Publishing Group	
Relação: 	http://archimer.ifremer.fr/doc/00000/6807/	
Formato: 	application/pdf	
Fonte: 	Embo Journal (0261-4189) (Nature Publishing Group), 2009-08 , Vol. 28 , N. 16 , P. 2479-2489	
Fonte: 	2009 European Molecular Biology Organization ; Nature