Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Sukhvinder Gill"'
Autor:
Aurore Gorlas, Pierre Jacquemot, Jean-Michel Guigner, Sukhvinder Gill, Patrick Forterre, François Guyot
Publikováno v:
PLoS ONE, Vol 13, Iss 8, p e0201549 (2018)
Interactions between hyperthermophilic archaea and minerals occur in hydrothermal deep-sea vents, one of the most extreme environments for life on Earth. These interactions occur in the internal pores and at surfaces of active hydrothermal chimneys.
Externí odkaz:
https://doaj.org/article/70811531a90a4e15975805c6d6bf7dfd
Publikováno v:
FEMS Microbiology Reviews
FEMS Microbiology Reviews, 2019, 43 (3), pp.273-303. ⟨10.1093/femsre/fuy042⟩
FEMS Microbiology Reviews, Wiley-Blackwell, 2019, 43 (3), pp.273-303. ⟨10.1093/femsre/fuy042⟩
FEMS Microbiology Reviews, 2019, 43 (3), pp.273-303. ⟨10.1093/femsre/fuy042⟩
FEMS Microbiology Reviews, Wiley-Blackwell, 2019, 43 (3), pp.273-303. ⟨10.1093/femsre/fuy042⟩
Cells from all three domains of life, Archaea, Bacteria and Eukarya, produce extracellular vesicles (EVs) which are sometimes associated with filamentous structures known as nanopods or nanotubes. The mechanisms of EV biogenesis in the three domains
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::be7be8f8487504c3e2801ac7fd92739d
https://hal.science/hal-02178889/file/fuy042.pdf
https://hal.science/hal-02178889/file/fuy042.pdf
Publikováno v:
Extremophiles
Extremophiles, Springer Verlag, 2015, 19 (1), pp.69-76. ⟨10.1007/s00792-014-0706-1⟩
Extremophiles, 2015, 19 (1), pp.69-76. ⟨10.1007/s00792-014-0706-1⟩
Extremophiles, Springer Verlag, 2015, 19 (1), pp.69-76. ⟨10.1007/s00792-014-0706-1⟩
Extremophiles, 2015, 19 (1), pp.69-76. ⟨10.1007/s00792-014-0706-1⟩
International audience; A combination of three enzymes from the hyperthermophilic archaeon Thermococcus nautili, DNA primase PolpTN2, DNA polymerase PolB, and pTN2 DNA helicase, was found to synthesize up to 300-400 ng/µl dsDNA from deoxynucleotide
Autor:
Patrick Forterre, Mart Krupovic, Nicole Desnoues, Sukhvinder Gill, Guennadi Sezonov, Pierre Béguin
Publikováno v:
Nucleic Acids Research
Nucleic Acids Research, Oxford University Press, 2014, 42 (6), pp.3707-3719. ⟨10.1093/nar/gkt1385⟩
Nucleic Acids Research, 2014, 42 (6), pp.3707-3719. ⟨10.1093/nar/gkt1385⟩
Nucleic Acids Research, Oxford University Press, 2014, 42 (6), pp.3707-3719. ⟨10.1093/nar/gkt1385⟩
Nucleic Acids Research, 2014, 42 (6), pp.3707-3719. ⟨10.1093/nar/gkt1385⟩
We report the characterization of a DNA primase/polymerase protein (PolpTN2) encoded by the pTN2 plasmid from Thermococcus nautilus. Sequence analysis revealed that this protein corresponds to a fusion between an N-terminal domain homologous to the s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4395e8244103bb1a036503b6a9c62219
https://hal.sorbonne-universite.fr/hal-01332620
https://hal.sorbonne-universite.fr/hal-01332620
Publikováno v:
Journal of molecular biology. 372(4)
The interaction of archaeal family B DNA polymerases with deaminated bases has been examined. As determined previously by our group, the polymerase binds tightly to uracil (the deamination product of cytosine), in single-stranded DNA, and stalls repl