Browsing Wieden, Hans-Joachim by Issue Date

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  • Juranek, Stefan; Wieden, Hans-Joachim; Lipps, Hans J. (Oxford University PressArts and ScienceDepartment of Chemistry and BiochemistryUniversity of Witten/HerdeckeUniversity of Lethbridgehttps://doi.org/10.1093/nar/gkg233, 2003)
    Dramatic DNA reorganization and elimination processes occur during macronuclear differentiation in ciliates. In this study we analyzed whether cytosine methylation of specific sequences plays a functional role during DNA ...
  • Gu, Shan-Qing; Peske, Frank; Wieden, Hans-Joachim; Rodnina, Marina V.; Wintermeyer, Wolfgang (Cold Springs Harbor Laboratory PressArts and ScienceDepartment of Chemistry and BiochemistryUniversity of Witten/HerdeckeUniversity of Lethbridgehttps://dx.doi.org/10.1261/rna.2196403, 2003)
    The signal recognition particle (SRP) from Escherichia coli, composed of Ffh protein and 4.5S RNA, mediates membrane targeting of translating ribosomes displaying a signal or signal-anchor sequence. SRP binds at the peptide ...
  • Friedt, Jenna; Leavens, Fern M. V.; Mercier, Evan; Wieden, Hans-Joachim; Wieden-Kothe, Ute (Oxford University PressArts and ScienceDepartment of Chemistry and BiochemistryMax Planck Institute for Biophysical ChemistryUniversity of Lethbridge, 2014)
    Pseudouridine synthases introduce the most common RNA modification and likely use the same catalytic mechanism. Besides a catalytic aspartate residue, the contributions of other residues for catalysis of pseudouridine ...
  • Tillault, Anne-Sophie; Fourmann, Jean-Baptiste; Loegler, Christine; Wieden, Hans-Joachim; Wieden-Kothe, Ute; Charpentier, Bruno (Cold Spring Harbor Laboratory PressArts and ScienceDepartment of Chemistry and BiochemistryBipole de l'Université de LorraineUniversity of Lethbridgehttps://dx.doi.org/10.1261/rna.051425.115, 2015)
    In all organisms, several distinct stand-alone pseudouridine synthase (PUS) family enzymes are expressed to isomerizeuridine into pseudouridine (Ψ) by specific recognition of RNAs. In addition, Ψs are generated in Archaea ...
  • De Laurentiis, Evelina I.; Mercier, Evan; Wieden, Hans-Joachim (American Society for Biochemistry and Molecular BiologyArts and ScienceDepartment of Chemistry and BiochemistryUniversity of Lethbridgehttps://dx.doi.org/10.1074/jbc.M116.740381, 2015)
    Little is known about the conservation of critical kinetic parameters and the mechanistic strategies of elongation factor (EF) Ts-catalyzed nucleotide exchange in EF-Tu in bacteria and particularly in clinically relevant ...
  • De Laurentiis, Evelina I.; Wieden, Hans-Joachim (Nature ResearchArts and ScienceDepartment of Chemistry and BiochemistryUniversity of Lethbridgehttps://dx.doi.org/10.1038/srep08573, 2015)
    The bacterial translational GTPase EF4/LepA is structurally similar to the canonical elongation factor EF-G. While sharing core structural features with other translational GTPases, the function of EF4 remains unknown. ...
  • Mercier, Evan; Girodat, Dylan; Wieden, Hans-Joachim (Nature ResearchArts and ScienceDepartment of Chemistry and BiochemistryUniversity of Lethbridgehttps://doi.org/10.1038/srep07677, 2015)
    The phosphate-binding loop (P-loop) is a conserved sequence motif found in mononucleotide-binding proteins. Little is known about the structural dynamics of this region and its contribution to the observed nucleotide binding ...
  • Coatham, Mackenzie L.; Brandon, Harland E.; Fischer, Jeffrey J.; Schummer, Tobias; Wieden, Hans-Joachim (Oxford University PressArts and ScienceDepartment of Chemistry and BiochemistryUniversity of AlbertaUniversity of Lethbridgehttps://doi.org/10.1093/nar/gkv1524, 2016)
    Using a combination of biochemical, structural probing and rapid kinetics techniques we reveal for the first time that the universally conserved translational GTPase (trGTPase) HflX binds to the E-site of the 70S ribosome ...
  • De Laurentiis, Evelina I.; Girodat, Dylan J.; Mercier, Evan; Wieden, Hans-Joachim (Biomath ForumArts and ScienceDepartment of Chemistry and BiochemistryUniversity of Lethbridgehttp://dx.doi.org/10.11145/bmc.2016.04.167, 2016)
    Translation, the ribosome dependent synthesis of proteins, is the last step of gene expression. It is targeted by a large number of antibiotics that modulate, in one way or the other, the dynamic properties of the involved ...
  • Beal, Jacob; Haddock-Angelli, Traci; Gershater, Markus; De Mora, Kim; Lizarazo, Meagan; Hollenhorst, Jim; Rettberg, Randy; iGEM Interlab Study Contributors (Public Library of ScienceArts and ScienceDepartment of Chemistry and BiochemistryRaytheon BBN TechnologiesiGEM FoundationSynthaceAgilentUniversity of Lethbridgehttps://dx.doi.org/10.1371/journal.pone.0150182, 2016)
    We present results of the first large-scale interlaboratory study carried out in synthetic biology, as part of the 2014 and 2015 International Genetically Engineered Machine (iGEM) competitions. Participants at 88 institutions ...
  • Gzyl, Katherine E.; Wieden, Hans-Joachim (Public Library of ScienceArts and ScienceDepartment of Chemistry and BiochemistryUniversity of Lethbridge, 2017)
    Understanding the molecular mechanism of antibiotics that are currently in use is important for the development of new antimicrobials. The tetracyclines, discovered in the 1940s, are a well-establis ...
  • Fernandes, Dennis D.; Bamrah, Jasbir; Kailasam, Senthilkumar; Gomes, Gregory-Neal W.; Li, Yuchong; Wieden, Hans-Joachim; Gradinaru, Claudiu C. (Nature ResearchArts and ScienceDepartment of Chemistry and BiochemistryUniversity of TorontoUniversity of Lethbridgehttps://doi.org/10.1038/s41598-017-13427-8, 2017)
    In recent years, new labelling strategies have been developed that involve the genetic insertion of small amino-acid sequences for specific attachment of small organic fluorophores. Here, we focus on the tetracysteine FCM ...
  • Tanzawa, Takehito; Kato, Koji; Girodat, Dylan; Ose, Toyoyuki; Kumakura, Yuki; Weiden, Hans-Joachim; Uchiumi, Toshio; Tanaka, Isao; Yao, Min (Oxford University PressArts and ScienceDepartment of Chemistry and BiochemistryHokkaido UniversityUniversity of LethbridgeNiigata Universityhttps://doi.org/10.1093/nar/gky115, 2018)
    Archaea and eukaryotes have ribosomal P stalks composed of anchor protein P0 and aP1 homodimers (archaea) or P1•P2 heterodimers (eukaryotes). These P stalks recruit translational GTPases to the GTPase-associated center in ...