Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Christiane Elie"'
Publikováno v:
Molecular Microbiology. 100:362-378
The Mre11:Rad50 complex is central to DNA double strand break repair in the Archaea and Eukarya, and acts through mechanical and nuclease activities regulated by conformational changes induced by ATP binding and hydrolysis. Despite the widespread use
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::80c71fb9854f767ce056f3977a640dde
https://doi.org/10.1111/mmi.13322
https://doi.org/10.1111/mmi.13322
Publikováno v:
Journal of Molecular Evolution. 45:107-114
We have isolated a new gene encoding a putative 103-kDa protein from the hyperthermophilic archaeon Sulfolobus acidocaldarius. Analysis of the deduced amino-acid sequence shows an extended central domain, predicted to form coiled-coil structures, and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ccb63f3f97c596a4ffadf0567db040d0
https://doi.org/10.1007/pl00006193
https://doi.org/10.1007/pl00006193
Autor:
M. Holmes, M. Dyall-Smith, Michel Duguet, F. Lottspeich, Patrick Forterre, Danièle Gadelle, A. Bergerat, Fabrice Confalonieri, Christiane Elie
Publikováno v:
Systematic and Applied Microbiology. 16:746-758
Summary We review our present knowledge on DNA topoisomerase and DNA polymerase evolution, with emphasis on information obtained by studying these enzymes in Archaea. Two archaeal DNA topoisomerase genes have been sequenced: the reverse gyrase from S
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7ae2142ebcdd15ec054eb77d0ad3e5f0
https://doi.org/10.1016/s0723-2020(11)80349-8
https://doi.org/10.1016/s0723-2020(11)80349-8
Autor:
Nadia Benachenhou-Lahfa, Michel Duguet, Bernard Labedan, Fabrice Confalonieri, Patrick Forterre, Christiane Elie
Publikováno v:
Biosystems. 28:15-32
The nature of the last universal ancestor to all extent cellular organisms and the rooting of the universal tree of life are fundamental questions which can now be adressed by molecular evolutionists. Several scenarios have been proposed during the l
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ed1644ae9ea762172825f7a7a33597d7
https://doi.org/10.1016/0303-2647(92)90004-i
https://doi.org/10.1016/0303-2647(92)90004-i
Publikováno v:
BMC Molecular Biology, Vol 9, Iss 1, p 25 (2008)
BMC Molecular Biology
BMC Molecular Biology, BioMed Central, 2008, 9 (1), pp.25. ⟨10.1186/1471-2199-9-25⟩
BMC Molecular Biology
BMC Molecular Biology, BioMed Central, 2008, 9 (1), pp.25. ⟨10.1186/1471-2199-9-25⟩
Background The ubiquitous Rad50 and Mre11 proteins play a key role in many processes involved in the maintenance of genome integrity in Bacteria and Eucarya, but their function in the Archaea is presently unknown. We showed previously that in most hy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::87f514cc4ea5cdfc7c1ca2c427ed901e
https://hdl.handle.net/10023/1027
https://hdl.handle.net/10023/1027
Autor:
Patrick Forterre, Anne-Marie de Recondo, Samia Salhi, Jean-Michel Rossignol, Olivier Jean-Jean, Michèle Meunier-Rotival, Christiane Elie
Publikováno v:
Biochemical and Biophysical Research Communications. 167:1341-1347
A DNA polymerase purified from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius was used to perform automated DNA amplification at 70 degrees C as well as site directed mutagenesis by Polymerase Chain Reaction (P.C.R.). The yield of am
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::847a48fdeaeb305d3c38f24955271023
https://doi.org/10.1016/0006-291x(90)90670-i
https://doi.org/10.1016/0006-291x(90)90670-i
Publikováno v:
European journal of biochemistry. 190(3)
A thermophilic DNA polymerase has been purified to near homogeneity from the archaebacterium Thermoplasma acidophilum. Analysis of the purified enzyme by sodium dodecyl sulfate gel electrophoresis revealed a single polypeptide of 88 kDa which co-sedi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::400adea4f41ee2e10c27b45efe7b4afc
https://pubmed.ncbi.nlm.nih.gov/2115439
https://pubmed.ncbi.nlm.nih.gov/2115439
Autor:
Fabrice Confalonieri, Christiane Elie, Marc Nadal, C B de la Tour, Michel Duguet, Patrick Forterre
Publikováno v:
Proceedings of the National Academy of Sciences. 91:3478-3478
Reverse gyrase is a type I DNA topoisomerase able to positively supercoil DNA and is found in thermophilic archaebacteria and eubacteria. The gene coding for this protein was cloned from Sulfolobus acidocaldarius DSM 639. Analysis of the 1247-amino a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a545502b3a291049109dd1007293941a
https://doi.org/10.1073/pnas.91.8.3478b
https://doi.org/10.1073/pnas.91.8.3478b
Publikováno v:
Journal of Molecular Biology. 209:635-644
The activity of a homogeneous DNA polymerase from the thermophilic archaebacterium, Sulfolobus acidocaldarius, on a singly primed, single-stranded recombinant phage M13 DNA has been examined. At the optimal temperature (70 to 75 degrees C) this templ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ab47f87192a03f42246964d3b392eb89
https://doi.org/10.1016/0022-2836(89)91000-0
https://doi.org/10.1016/0022-2836(89)91000-0
Publikováno v:
European Journal of Biochemistry. 178:619-626
We have purified to near homogeneity a DNA polymerase from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius. Sodium dodecyl sulfate gel electrophoresis of the purified enzyme revealed a polypeptide of 100 kDa. On the basis of a Stokes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ac61d3ce706df4371ac83008c90585a6
https://doi.org/10.1111/j.1432-1033.1989.tb14490.x
https://doi.org/10.1111/j.1432-1033.1989.tb14490.x