Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Ursula Aschke-Sonnenborn"'
Autor:
Birgit Klinkert, Jens Kortmann, Franz Narberhaus, Friederike M Kaiser, Ursula Aschke-Sonnenborn, Annika Cimdins
Publikováno v:
RNA Biology
Cyanobacteria constitute a heterogeneous phylum of oxygen-producing, photosynthetic prokaryotes. They are susceptible to various stress conditions like heat, salt, or light stress, all inducing the cyanobacterial heat shock response (HSR). Cyanobacte
Autor:
Franz Narberhaus, Birgit Klinkert, Ursula Aschke-Sonnenborn, Annika Cimdins, Johanna Roßmanith, Lena C. Gaubig
Publikováno v:
Journal of Biotechnology. 160:55-63
Free-living bacteria constantly monitor their ambient temperature. Drastic deviations elicit immediate protective responses known as cold shock or heat shock response. Many mammalian pathogens use temperature surveillance systems to recognize the suc
Autor:
Wolfgang Rüger, Paul S. Freemont, Laurent Larivière, Solange Moréra, Ursula Aschke-Sonnenborn, Joël Janin, Jürgen Kurzeck
Publikováno v:
Journal of Molecular Biology. 311:569-577
β-Glucosyltransferase (BGT) is a DNA-modifying enzyme encoded by bacteriophage T4 that transfers glucose from uridine diphosphoglucose to 5-hydroxymethyl cytosine bases of phage T4 DNA. We report six X-ray structures of the substrate-free and the UD
Publikováno v:
Journal of Molecular Biology. 292:717-730
β-Glucosyltransferase (BGT) is a DNA-modifying enzyme encoded by bacteriophage T4 which catalyses the transfer of glucose (Glc) from uridine diphosphoglucose (UDP-Glc) to 5-hydroxymethylcytosine (5-HMC) in double-stranded DNA. The glucosylation of T
Publikováno v:
Acta crystallographica. Section D, Biological crystallography. 58(Pt 9)
A base-flipping phenomenon has been established for DNA methyltransferases and for DNA base-excision repair glycosylases and is likely to prove general for enzymes that need access to DNA bases to undergo chemical reaction. T4 phage beta-glucosyltran