Consulta: creatorFacets:"Myllykallio, Hannu"
Registros recuperados: 2
Data/hora: 06/06/2024 17:02:53

A novel proteomic approach identifies new interaction partners for proliferating cell nuclear antigen
Provedor de dados: 5
Autores: Mesiet Cladiere, L; Norais, Cédric; Kuhn, Joelle; Briffotaux, Julien; Sloostra, Jerry W.; Ferrari, Elena; Hubscher, Ulrich; Flament, Didier; Myllykallio, Hannu.
During DNA replication and repair, many proteins bind to and dissociate in a highly specific and ordered manner from proliferating cell nuclear antigen (PCNA). We describe a combined approach of in silico searches at the genome level and combinatorial peptide synthesis to investigate the binding properties of hundreds of short PCNA-interacting peptides (PIP-peptides) to archaeal and eukaryal PCNAs. Biological relevance of our combined approach was demonstrated by identification an inactive complex of Pyrococcus abyssi ribonuclease HII with PCNA. Furthermore we show that PIP-peptides interact with PCNA largely in a sequence independent manner. Our experimental approach also identified many so far unidentified PCNA interacting peptides in a number of human...
Tipo: Text
Palavras-chave: Ribonuclease HII; Combinatorial peptide synthesis; PCNA.
Ano: 2007
URL: http://archimer.ifremer.fr/doc/2007/publication-3297.pdf

Structure and function of a novel endonuclease acting on branched DNA substrates
Provedor de dados: 5
Autores: Ren, Bin; Kuehn, Joelle; Meslet-cladiere, Laurence; Briffotaux, Julien; Norais, Cedric; Lavigne, Regis; Flament, Didier; Ladenstein, Rudolf; Myllykallio, Hannu.
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...
Tipo: Text
Palavras-chave: Structure function studies; RecB family; Novel endonuclease; DNA repair; Branched DNA structures.
Ano: 2009
URL: http://archimer.ifremer.fr/doc/2009/publication-6807.pdf