نتایج جستجو برای: ralstonia eutropha h16

تعداد نتایج: 2604  

Journal: :Applied and environmental microbiology 2011
Matthias Raberg Katja Peplinski Silvia Heiss Armin Ehrenreich Birgit Voigt Christina Döring Mechthild Bömeke Michael Hecker Alexander Steinbüchel

By taking advantage of the available genome sequence of Ralstonia eutropha H16, glucose uptake in the UV-generated glucose-utilizing mutant R. eutropha G(+)1 was investigated by transcriptomic and proteomic analyses. Data revealed clear evidence that glucose is transported by a usually N-acetylglucosamine-specific phosphotransferase system (PTS)-type transport system, which in this mutant is pr...

Journal: :Applied and environmental microbiology 2015
Anna Sznajder Daniel Pfeiffer Dieter Jendrossek

Identification of proteins that were present in a polyhydroxybutyrate (PHB) granule fraction isolated from Ralstonia eutropha but absent in the soluble, membrane, and membrane-associated fractions revealed the presence of only 12 polypeptides with PHB-specific locations plus 4 previously known PHB-associated proteins with multiple locations. None of the previously postulated PHB depolymerase is...

Journal: :Applied and environmental microbiology 2013
Jana Müller Daniel MacEachran Helcio Burd Noppadon Sathitsuksanoh Changhao Bi Yi-Chun Yeh Taek Soon Lee Nathan J Hillson Swapnil R Chhabra Steven W Singer Harry R Beller

Ralstonia eutropha is a facultatively chemolithoautotrophic bacterium able to grow with organic substrates or H2 and CO2 under aerobic conditions. Under conditions of nutrient imbalance, R. eutropha produces copious amounts of poly[(R)-3-hydroxybutyrate] (PHB). Its ability to utilize CO2 as a sole carbon source renders it an interesting new candidate host for the production of renewable liquid ...

Journal: :Biochemical Society transactions 2006
R Cramm A Büsch K Strube

The sigma54-dependent transcriptional regulator NorR of Ralstonia eutropha H16 activates gene expression in response to nitric oxide (NO). The N-terminal domain of NorR is thought to be involved in signal perception. A C112S exchange within this domain abolished promoter activation by the mutated protein, indicating that Cys(112) is essential for the signalling mechanism of NorR. The DNA region...

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