Výsledky vyhledávání - "Sonja Hasenbein"

Co-ordinated regulation of gluconate catabolism and glucose uptake in Corynebacterium glutamicum by two functionally equivalent transcriptional regulators, GntR1 and GntR2

Autor: Julia Frunzke, Sonja Hasenbein, Cornelia Gätgens, Verena Engels, Michael Bott

Publikováno v: Molecular Microbiology. 67:305-322

Corynebacterium glutamicum is a Gram-positive soil bacterium that prefers the simultaneous catabolism of different carbon sources rather than their sequential utilization. This type of metabolism requires an adaptation of the utilization rates to the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::2e6b69afeba071cd3c4605453cb06e21
https://doi.org/10.1111/j.1365-2958.2007.06020.x

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Structure of the full-length HPr kinase/phosphatase from Staphylococcus xylosus at 1.95 Å resolution: Mimicking the product/substrate of the phospho transfer reactions

Autor: Brigitte Koch, Sonia Fieulaine, Wolfgang Hengstenberg, José A. Márquez, Sonja Hasenbein, Klaus Scheffzek, Robert B. Russell, Sylvie Nessler

Publikováno v: Proceedings of the National Academy of Sciences. 99:3458-3463

The histidine containing phospho carrier protein (HPr) kinase/phosphatase is involved in carbon catabolite repression, mainly in Gram-positive bacteria. It is a bifunctional enzyme that phosphorylates Ser-46-HPr in an ATP-dependent reaction and depho

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aa50509f5808b076572387c981c91d01
https://doi.org/10.1073/pnas.052461499

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Conversion of a regulatory into a degradative protease

Autor: Tim Clausen, Michael Meltzer, Patrick Hauske, Robert Huber, Michael Ehrmann, Sonja Hasenbein, Markus Kaiser

The PDZ protease DegS senses mislocalized outer membrane proteins and initiates the sigmaE pathway in the bacterial periplasm. This unfolded protein response pathway is activated by processing of the anti-sigma factor RseA by DegS and other proteases

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::07c3b9d7a804c7690c3f7dfe884fa8f5
https://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&origin=inward&scp=77950020354

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Transcriptional control of the succinate dehydrogenase operon sdhCAB of Corynebacterium glutamicum by the cAMP-dependent regulator GlxR and the LuxR-type regulator RamA

Autor: Michael Bott, Sabine Degraf, Michael Bussmann, Sonja Hasenbein, Denise Emer, Bernhard J. Eikmanns

Publikováno v: Journal of biotechnology. 143(3)

In experiments performed to identify transcriptional regulators of the tricarboxylic acid cycle of Corynebacterium glutamicum, the cAMP-dependent regulator GlxR and the regulators of acetate metabolism RamA and RamB were enriched by DNA affinity chro

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::82b20f803e7176e2fdd569163c9585c2
https://pubmed.ncbi.nlm.nih.gov/19583988

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Structure, function and regulation of the conserved serine proteases DegP and DegS of Escherichia coli

Autor: Michael Ehrmann, Tim Clausen, Patrick Hauske, Nicolette Mamant, T. Krojer, Melisa Merdanovic, Simon Poepsel, Robert Huber, Markus Kaiser, Sonja Hasenbein, Michael Meltzer

Two members of the widely conserved HtrA family of serine proteases, DegP and DegS, are key players in extracytoplasmic protein quality control. The underlying mechanisms of their main functions in stress sensing, regulation and protection during the

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Allosteric activation of HtrA protease DegP by stress signals during bacterial protein quality control

Autor: T. Krojer, D. Dafydd Jones, Nicolette Kucz, Sonja Hasenbein, Markus Kaiser, Sandra Grau, Tim Clausen, Melisa Merdanovic, Patrick Hauske, Michael Ehrmann, Alexandra Beil, Michael Meltzer

Publikováno v: Angewandte Chemie (International ed. in English). 47(7)

Unleashing the proteolytic activity of DegP: A study with synthetic mimics of cellular stress signals reveals an allosteric (chemical) activation mechanism of the bacterial HtrA protease DegP, leading to a fine-tuned amplification of protein degradat

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::740760d93edb7942a5f735cc79953311
https://pubmed.ncbi.nlm.nih.gov/18175296

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Determinants of regulated proteolysis in signal transduction

Autor: Melisa Merdanovic, Sonja Hasenbein, Michael Ehrmann

Each cell produces thousands of gene products that differ in cellular localization, chemical properties, interactions with other cellular factors, abundance, and half lives. Controlling these events presents an enormous organizational challenge. In r

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Regulation of the σE stress response by DegS: How the PDZ domain keeps the protease inactive in the resting state and allows integration of different OMP-derived stress signals upon folding stress

Autor: Tim Clausen, Michael Ehrmann, Juliane Kurt, T. Krojer, Sonja Hasenbein, Corinna Wilken, Justyna Sawa, Hanna Hasselblatt, Robert Kurzbauer, Rebecca Kirk

The unfolded protein response of Escherichia coli is triggered by the accumulation of unassembled outer membrane proteins (OMPs) in the cellular envelope. The PDZ-protease DegS recognizes these mislocalized OMPs and initiates a proteolytic cascade th

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High-resolution structure of the histidine-containing phosphocarrier protein (HPr) from Staphylococcus aureus and characterization of its interaction with the bifunctional HPr kinase/phosphorylase

Autor: Hans Robert Kalbitzer, Wolfgang Hengstenberg, Norman Kachel, Sonja Hasenbein, Till Maurer, Claudia Elisabeth Munte, Sebastian Meier, Brigitte Koch

Publikováno v: Journal of bacteriology 186, 5906-5918 (2004). doi:10.1128/JB.186.17.5906-5918.2004

A high-resolution structure of the histidine-containing phosphocarrier protein (HPr) from Staphylococcus aureus was obtained by heteronuclear multidimensional nuclear magnetic resonance (NMR) spectroscopy on the basis of 1,766 structural restraints.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d298197bd59a0871ac4620f7977bf723
https://pubmed.ncbi.nlm.nih.gov/15317796

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