Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Stephen Douthwaite"'
Autor:
Stephen Douthwaite, Finn Kirpekar, Jesper F. Havelund, Simon Rose, Harald Huber, Sylvie Auxilien, Henri Grosjean
Publikováno v:
Nucleic Acids Research
Nucleic Acids Research, 2020, 48 (12), pp.6906--6918. ⟨10.1093/nar/gkaa411⟩
Rose, S, Auxilien, S, Havelund, J F, Kirpekar, F, Huber, H, Grosjean, H & Douthwaite, S 2020, ' The hyperthermophilic partners Nanoarchaeum and Ignicoccus stabilize their tRNA T-loops via different but structurally equivalent modifications ', Nucleic acids research, vol. 48, no. 12, pp. 6906-6918 . https://doi.org/10.1093/nar/gkaa411
Nucleic Acids Research, 2020, 48 (12), pp.6906--6918. ⟨10.1093/nar/gkaa411⟩
Rose, S, Auxilien, S, Havelund, J F, Kirpekar, F, Huber, H, Grosjean, H & Douthwaite, S 2020, ' The hyperthermophilic partners Nanoarchaeum and Ignicoccus stabilize their tRNA T-loops via different but structurally equivalent modifications ', Nucleic acids research, vol. 48, no. 12, pp. 6906-6918 . https://doi.org/10.1093/nar/gkaa411
Place: Oxford Publisher: Oxford Univ Press WOS:000574288800042; The universal L-shaped tertiary structure of tRNAs is maintained with the help of nucleotide modifications within the D- and T-loops, and these modifications are most extensive within hy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::78b76e995c76b279dd947f01251ee9ff
https://hal.archives-ouvertes.fr/hal-02968376
https://hal.archives-ouvertes.fr/hal-02968376
Autor:
Laure Béven, Djemel Hamdane, Catherine Goyenvalle, Simon Rose, Henri Grosjean, Damien Brégeon, Alain Blanchard, Stephen Douthwaite, Pascal Sirand-Pugnet, Valérie de Crécy-Lagard
Publikováno v:
Biomolecules
Biomolecules, MDPI, 2020, 10 (4), pp.587. ⟨10.3390/biom10040587⟩
Biomolecules, 2020, 10 (4), pp.587. ⟨10.3390/biom10040587⟩
Sirand-Pugnet, P, Brégeon, D, Béven, L, Goyenvalle, C, Blanchard, A, Rose, S, Grosjean, H, Douthwaite, S, Hamdane, D & Crécy-Lagard, V D 2020, ' Reductive Evolution and Diversification of C5-Uracil Methylation in the Nucleic Acids of Mollicutes ', Biomolecules, vol. 10, no. 4, 587 . https://doi.org/10.3390/biom10040587
Volume 10
Issue 4
Biomolecules, Vol 10, Iss 587, p 587 (2020)
Biomolecules, MDPI, 2020, 10 (4), pp.587. ⟨10.3390/biom10040587⟩
Biomolecules, 2020, 10 (4), pp.587. ⟨10.3390/biom10040587⟩
Sirand-Pugnet, P, Brégeon, D, Béven, L, Goyenvalle, C, Blanchard, A, Rose, S, Grosjean, H, Douthwaite, S, Hamdane, D & Crécy-Lagard, V D 2020, ' Reductive Evolution and Diversification of C5-Uracil Methylation in the Nucleic Acids of Mollicutes ', Biomolecules, vol. 10, no. 4, 587 . https://doi.org/10.3390/biom10040587
Volume 10
Issue 4
Biomolecules, Vol 10, Iss 587, p 587 (2020)
The C5-methylation of uracil to form 5-methyluracil (m5U) is a ubiquitous base modification of nucleic acids. Four enzyme families have converged to catalyze this methylation using different chemical solutions. Here, we investigate the evolution of 5
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3cd5987e6d5773d0f47a19ceee3ec349
https://hal.archives-ouvertes.fr/hal-02547879
https://hal.archives-ouvertes.fr/hal-02547879
Autor:
Stephen Douthwaite, Henrik Nielsen, Simon Rose, Kenneth H Seistrup, Harald Huber, Ulf Birkedal
Publikováno v:
Seistrup, K H, Rose, S, Birkedal, U, Nielsen, H, Huber, H & Douthwaite, S 2017, ' Bypassing rRNA methylation by RsmA/Dim1during ribosome maturation in the hyperthermophilic archaeon Nanoarchaeum equitans ', Nucleic Acids Research, vol. 45, no. 4, pp. 2007-2015 . https://doi.org/10.1093/nar/gkw839
Nucleic Acids Research
Nucleic Acids Research
In all free-living organisms a late-stage checkpoint in the biogenesis of the small ribosomal subunit involves rRNA modification by an RsmA/Dim1 methyltransferase. The hyperthermophilic archaeon Nanoarchaeum equitans, whose existence is confined to t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::df266633403113ec7bc02338a035aaa2
https://findresearcher.sdu.dk:8443/ws/files/135012733/Bypassing_rRNA_methylation_by_RsmA_Dim1during_ribosome_maturation_in_the_hyperthermophilic_archaeon_Nanoarchaeum_equitans.pdf
https://findresearcher.sdu.dk:8443/ws/files/135012733/Bypassing_rRNA_methylation_by_RsmA_Dim1during_ribosome_maturation_in_the_hyperthermophilic_archaeon_Nanoarchaeum_equitans.pdf
Publikováno v:
Madsen, C T, Mengel-From, J, Kirpekar, F & Douthwaite, S 2003, ' Identifying the methyltransferases for m5U747 and m5U1939 in 23S rRNA using MALDI mass spectrometry ', Nucleic Acids Research, vol. 31, pp. 4738-46 . https://doi.org/10.1093/nar/gkg657
There are three sites of m(5)U modification in Escherichia coli stable RNAs: one at the invariant tRNA position U54 and two in 23S rRNA at the phylogenetically conserved positions U747 and U1939. Each of these sites is modified by its own methyltrans
Autor:
Simon Rose, Alain Blanchard, Stephen Douthwaite, Henri Grosjean, Anne Lebaudy, Basma El Yacoubi, Carole Lartigue
Publikováno v:
Nucleic Acids Research
Nucleic Acids Research, Oxford University Press, 2014, 42 (12), pp.8073-8082. ⟨10.1093/nar/gku518⟩
Lartigue, C, Lebaudy, A, Blanchard, A, El Yacoubi, B, Rose, S, Grosjean, H & Douthwaite, S R 2014, ' The flavoprotein Mcap0476 (RlmFO) catalyzes m5U1939 modification in Mycoplasma capricolum 23S rRNA ', Nucleic Acids Research, vol. 42, no. 12, pp. 8073-82 . https://doi.org/10.1093/nar/gku518
Nucleic Acids Research 12 (42), 8073-8082. (2014)
Nucleic Acids Research, Oxford University Press, 2014, 42 (12), pp.8073-8082. ⟨10.1093/nar/gku518⟩
Lartigue, C, Lebaudy, A, Blanchard, A, El Yacoubi, B, Rose, S, Grosjean, H & Douthwaite, S R 2014, ' The flavoprotein Mcap0476 (RlmFO) catalyzes m5U1939 modification in Mycoplasma capricolum 23S rRNA ', Nucleic Acids Research, vol. 42, no. 12, pp. 8073-82 . https://doi.org/10.1093/nar/gku518
Nucleic Acids Research 12 (42), 8073-8082. (2014)
International audience; Efficient protein synthesis in all organisms requires the post-transcriptional methylation of specific ribosomal ribonucleic acid (rRNA) and transfer RNA (tRNA) nucleotides. The methylation reactions are almost invariably cata
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::af7d66b5720d4378fdec912f63de6fd7
https://hal.inrae.fr/hal-02640441
https://hal.inrae.fr/hal-02640441
Autor:
Benoît Desmolaize, Patrice Courvalin, Marc Galimand, Yves Mechulam, Michel Panvert, Emmanuelle Schmitt, Stephen Douthwaite
Publikováno v:
RNA
RNA, Cold Spring Harbor Laboratory Press, 2011, 17 (2), pp.251-62. ⟨10.1261/rna.2233511⟩
RNA, 2011, 17 (2), pp.251-62. ⟨10.1261/rna.2233511⟩
Galimand, M, Schmitt, E, Panvert, M, Desmolaize, B, Douthwaite, S R, Mechulam, Y & Courvalin, P 2011, ' Intrinsic resistance to aminoglycosides in Enterococcus faecium is conferred by the 16S rRNA m5C1404-specific methyltransferase EfmM ', R N A, vol. 17, no. 2, pp. 251-62 . https://doi.org/10.1261/rna.2233511
RNA, Cold Spring Harbor Laboratory Press, 2011, 17 (2), pp.251-62. ⟨10.1261/rna.2233511⟩
RNA, 2011, 17 (2), pp.251-62. ⟨10.1261/rna.2233511⟩
Galimand, M, Schmitt, E, Panvert, M, Desmolaize, B, Douthwaite, S R, Mechulam, Y & Courvalin, P 2011, ' Intrinsic resistance to aminoglycosides in Enterococcus faecium is conferred by the 16S rRNA m5C1404-specific methyltransferase EfmM ', R N A, vol. 17, no. 2, pp. 251-62 . https://doi.org/10.1261/rna.2233511
Aminoglycosides are ribosome-targeting antibiotics and a major drug group of choice in the treatment of serious enterococcal infections. Here we show that aminoglycoside resistance in Enterococcus faecium strain CIP 54-32 is conferred by the chromoso
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e0cf8cbd11476355b4677727af1fcd83
https://hal-polytechnique.archives-ouvertes.fr/hal-00764856
https://hal-polytechnique.archives-ouvertes.fr/hal-00764856
Autor:
Sylvie Auxilien, Céline Brochier-Armanet, Simon Rose, Stephen Douthwaite, Clotilde Husson, Henri Grosjean, Anette Rasmussen, Dominique Fourmy
Publikováno v:
RNA
RNA, Cold Spring Harbor Laboratory Press, 2011, 17 (1), pp.45-53. ⟨10.1261/rna.2323411⟩
Auxilien, S, Rasmussen, A, Rose, S, Brochier-Armanet, C, Husson, C, Fourmy, D, Grosjean, H & Douthwaite, S R 2011, ' Specificity shifts in the rRNA and tRNA nucleotide targets of archaeal and bacterial m5U methyltransferases ', R N A, vol. 17, no. 1, pp. 45-53 . https://doi.org/10.1261/rna.2323411
RNA, Cold Spring Harbor Laboratory Press, 2011, 17 (1), pp.45-53. ⟨10.1261/rna.2323411⟩
Auxilien, S, Rasmussen, A, Rose, S, Brochier-Armanet, C, Husson, C, Fourmy, D, Grosjean, H & Douthwaite, S R 2011, ' Specificity shifts in the rRNA and tRNA nucleotide targets of archaeal and bacterial m5U methyltransferases ', R N A, vol. 17, no. 1, pp. 45-53 . https://doi.org/10.1261/rna.2323411
Methyltransferase enzymes that use S-adenosylmethionine as a cofactor to catalyze 5-methyl uridine (m5U) formation in tRNAs and rRNAs are widespread in Bacteria and Eukaryota, but are restricted to the Thermococcales and Nanoarchaeota groups amongst
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5e537a57003667278300b99b45f5ef3f
https://hal.archives-ouvertes.fr/hal-00580893
https://hal.archives-ouvertes.fr/hal-00580893
Autor:
Toni Gabaldón, Magda Villarroya, Stephen Douthwaite, M.-Eugenia Armengod, Alfonso Benítez-Páez
Publikováno v:
Benítez-Páez, A, Villarroya, M, Douthwaite, S R, Gabaldón, T & Armengod, M-E 2010, ' YibK is the 2'-O-methyltransferase TrmL that modifies the wobble nucleotide in Escherichia coli tRNA(Leu) isoacceptors ', R N A, vol. 16, no. 11, pp. 2131-43 . https://doi.org/10.1261/rna.2245910
Transfer RNAs are the most densely modified nucleic acid molecules in living cells. In Escherichia coli, more than 30 nucleoside modifications have been characterized, ranging from methylations and pseudouridylations to more complex additions that re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::df4b49b47c2beadc3a245d701454cf3b
https://portal.findresearcher.sdu.dk/da/publications/cb669500-0e27-421d-a7f8-e7490bb2c3cc
https://portal.findresearcher.sdu.dk/da/publications/cb669500-0e27-421d-a7f8-e7490bb2c3cc
Publikováno v:
Auxilien, S, El Khadali, F, Rasmussen, A, Douthwaite, S & Grosjean, H 2007, ' Archease from Pyrococcus abyssi improves substrate specificity and solubility of a tRNA m5C methyltransferase ', Journal of Biological Chemistry, vol. 282, no. 26, pp. 18711-18721 . https://doi.org/10.1074/jbc.M607459200
Udgivelsesdato: 2007-Jun-29 Members of the archease superfamily of proteins are represented in all three domains of life. Archease genes are generally located adjacent to genes encoding proteins involved in DNA or RNA processing. Archease have theref
Autor:
Dominique Fourmy, Stephen Douthwaite, Anne R. Stenholm, Eric Guittet, Isabelle Lebars, Satoko Yoshizawa
Publikováno v:
Lebars, I, Yoshizawa, S, Stenholm, A R, Guittet, E, Douthwaite, S & Fourmy, D 2003, ' Structure of 23S ribosomal RNA hairpin 35 and its interaction with the tylosin-resistance methyltransferase RlmAII ', EMBO Journal, vol. 22, no. 2, pp. 183-92 . https://doi.org/10.1093/emboj/cdg022
The bacterial rRNA methyltransferase RlmAII (formerly TlrB) contributes to resistance against tylosin-like 16-membered ring macrolide antibiotics. RlmAII was originally discovered in the tylosin-producer Streptomyces fradiae, and members of this subc