| Registro completo |
| Provedor de dados: |
ArchiMer
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| País: |
France
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| Título: |
Role of RadA and DNA Polymerases in Recombination-Associated DNA Synthesis in Hyperthermophilic Archaea
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| Autores: |
Hogrel, Gaelle
Lu, Yang
Alexandre, Nicolas
Bossé, Audrey
Dulermo, Remi
Ishino, Sonoko
Ishino, Yoshizumi
Flament, Didier
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| Data: |
2020-07
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| Ano: |
2020
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| Palavras-chave: |
Homologous recombination
Archaea
DNA polymerase
Recombinase
DNA repair
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| Resumo: |
Among the three domains of life, the process of homologous recombination (HR) plays a central role in the repair of double-strand DNA breaks and the restart of stalled replication forks. Curiously, main protein actors involved in the HR process appear to be essential for hyperthermophilic Archaea raising interesting questions about the role of HR in replication and repair strategies of those Archaea living in extreme conditions. One key actor of this process is the recombinase RadA, which allows the homologous strand search and provides a DNA substrate required for following DNA synthesis and restoring genetic information. DNA polymerase operation after the strand exchange step is unclear in Archaea. Working with Pyrococcus abyssi proteins, here we show that both DNA polymerases, family-B polymerase (PolB) and family-D polymerase (PolD), can take charge of processing the RadA-mediated recombination intermediates. Our results also indicate that PolD is far less efficient, as compared with PolB, to extend the invaded DNA at the displacement-loop (D-loop) substrate. These observations coincide with previous genetic analyses obtained on Thermococcus species showing that PolB is mainly involved in DNA repair without being essential probably because PolD could take over combined with additional partners.
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| Tipo: |
Text
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| Idioma: |
Inglês
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| Identificador: |
https://archimer.ifremer.fr/doc/00641/75274/75539.pdf
https://archimer.ifremer.fr/doc/00641/75274/75540.pdf
DOI:10.3390/biom10071045
https://archimer.ifremer.fr/doc/00641/75274/
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| Editor: |
MDPI AG
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| Formato: |
application/pdf
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| Fonte: |
Biomolecules (2218-273X) (MDPI AG), 2020-07 , Vol. 10 , N. 7 , P. 1045 (17p.)
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| Direitos: |
info:eu-repo/semantics/openAccess
restricted use
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