Stable interactions between DNA polymerase δ catalytic and structural subunits are essential for efficient DNA repair

Autor: Laurent Maloisel, Serge Gangloff, Jean-Baptiste Charbonnier, Clémentine Brocas, Claudine Dherin

Publikováno v: DNA Repair
DNA Repair, Elsevier, 2010, 9 (10), pp.1098-1111. ⟨10.1016/j.dnarep.2010.07.013⟩
DNA Repair, 2010, 9 (10), pp.1098-1111. ⟨10.1016/j.dnarep.2010.07.013⟩

International audience; Eukaryotic DNA polymerase δ (Pol δ) activity is crucial for chromosome replication and DNA repair and thus, plays an essential role in genome stability. In Saccharomyces cerevisiae, Pol δ is a heterotrimeric complex compose

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8f116a81d23d7979112dfe943b83bbf7
https://doi.org/10.1016/j.dnarep.2010.07.013

Sequential recruitment of the repair factors during NER: the role of XPG in initiating the resynthesis step

Autor: Zhou Yajin, Thilo Riedl, Jean-Marc Egly, Marietta Y.W.T. Lee, Jean Philippe Lainé, Vincent Mocquet

Publikováno v: EMBO Journal
EMBO Journal, EMBO Press, 2008, 27 (1), pp.155-67. ⟨10.1038/sj.emboj.7601948⟩

To address the biochemical mechanisms underlying the coordination between the various proteins required for nucleotide excision repair (NER), we employed the immobilized template system. Using either wild-type or mutated recombinant proteins, we iden

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d717ddd16f9b17a49ce1f8b162ceb40c
https://doi.org/10.1038/sj.emboj.7601948

DNA replication defects in a mutant deficient in the thioredoxin homolog YbbN

Autor: Gilbert Richarme, Hai Tuong Le, Masamichi Kohiyama, Tsutomu Katayama, Fatoum Kthiri, Valérie Gautier

Publikováno v: Biochemical and Biophysical Research Communications
Biochemical and Biophysical Research Communications, Elsevier, 2011, 405 (1), pp.52-7. ⟨10.1016/j.bbrc.2010.12.122⟩

International audience; Escherichia coli contains two thioredoxins, Trx1 and Trx2, and a thioredoxin-like protein, YbbN, that displays both redox and chaperone properties. Since three out of the six proteins of the YbbN interactome (Butland et al., 2

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::30698060fd9e213ae3dccf0451b21bf8
https://hal.archives-ouvertes.fr/hal-00588001

Phosphorylation of the C subunit (p66) of human DNA polymerase delta

Autor: Giuseppe Baldacci, Patrick Hughes, Claude Cochet, Serge Urbach, Laure Lemmens, Renaud Prudent

Publikováno v: Biochemical and Biophysical Research Communications
Biochemical and Biophysical Research Communications, Elsevier, 2008, 367 (2), pp.264-70. ⟨10.1016/j.bbrc.2007.12.083⟩
Biochemical and Biophysical Research Communications, 2008, 367 (2), pp.264-70. ⟨10.1016/j.bbrc.2007.12.083⟩

International audience; Of the four subunits constituting DNA polymerase delta, subunit C or p66 has been shown to mainly mediate polymerase interaction with PCNA, an auxiliary factor that greatly enhances DNA polymerase delta processivity on primed

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7a581ff1dd62c32dec547e816894ce4b
https://www.hal.inserm.fr/inserm-00413493

Distinct pools of proliferating cell nuclear antigen associated to DNA replication sites interact with the p125 subunit of DNA polymerase delta or DNA ligase I

Autor: Federica Riva, Ornella Cazzalini, Bernard Ducommun, Ennio Prosperi, Ivana Scovassi, Monica Savio, Lucia Anna Stivala, Lynne S. Cox

Publikováno v: Experimental Cell Research
Experimental Cell Research, Elsevier, 2004, 293 (2), pp.357-67

Proliferating cell nuclear antigen (PCNA) plays an essential role in DNA replication, repair, and cell cycle control. PCNA is a homotrimeric ring that, when encircling DNA, is not easily extractable. Consequently, the dynamics of protein-protein inte

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::65d0684560492978265a8352755a8532
https://pubmed.ncbi.nlm.nih.gov/14729473