1st Umeå Interdisciplinary Symposium on Hypoxic Biology - 25 May 8:45-16:45, online via Zoom

Details: Created: Monday, 26 April 2021 06:27

The concentration of oxygen is one of the most important variables in many physiological and pathological processes. Do you care about oxygen levels in your experiments? Probably you should, and now you can at UHRF.

UHRF (Umeå Hypoxia Research Facility) is a new facility created to support research projects that require controlled oxygen conditions. We are co-financed by the Kempe Foundation and the Umeå Center for Microbial Research (UCMR) and you can find us at the Department of Molecular Biology.

To introduce UHRF, we have organized an exciting virtual symposium to highlight the fundamental role of hypoxia in microbial ecology and infection, fungal biology, plant science, cancer, neurobiology and virology research. This first interdisciplinary symposium on hypoxic biology in Umeå is a joint initiative of UHRF (https://www.umu.se/en/uhrf) and UCMR (https://www.ucmr.umu.se/).

The invited speakers include: Michael Jetten (Microbial ecology; Radboud University, The Netherlands), Emilio Bueno (Infection biology; University of Umeå, Sweden), Francesco Licausi (Plant biology; University of Oxford, UK), Emily Flashman (Plant biology; University of Oxford, UK) Jonathan Gilthorpe (Neurobiology; University of Umeå, Sweden), Randall Johnson (Tumor biology; Karolinska institutet, Sweden), Jane McKeating (Virology; University of Oxford, UK), Robert A. Cramer (Fungal biology; Geisel School of Medicine, USA), Constantin Urban (Fungal biology; University of Umeå, Sweden), Björn Schröder (Gut microbiome; University of Umeå, Sweden), Andreas Baumler (Gut microbiome; UCDAVIS, USA).

Program:

https://www.umu.se/globalassets/centralwebb/forskningswebb/infrastruktur/uhrf/uhrf-symposium-programme-1.pdf

https://www.umu.se/en/research/infrastructure/umea-hypoxic-research-facility/uhrf-courses-and-events/

For questions contact: This email address is being protected from spambots. You need JavaScript enabled to view it.; This email address is being protected from spambots. You need JavaScript enabled to view it.

Nobel Prize in Chemistry 2020 to Emmanuelle Charpentier

Details: Created: Wednesday, 07 October 2020 13:54

UCMR Alumna Emmanuelle Charpentier

Awarded Nobel Prize in Chemisty 2020

Emmanuelle Charpentier, Max Planck Unit for the Science of Pathogens, Berlin, Germany, and Jennifer A. Doudna University of California, Berkeley, USA, receive the Nobel Prize in Chemisty for "developing a method of genome editing".

Emmanuelle Charpentier was one of the first recruited group leaders at the Laboratory for Molecular Infection Medicine Sweden, MIMS, within the Umeå Centre for Microbial Research (UCMR) at Umeå University. During Emmanuelle Charpentier’s studies on Streptococcus pyogenes, she discovered a new molecule, tracrRNA, which together with CRISPR RNA and Cas9 play an important role in activation of the CRISPR-Cas system's defense mechanism in the pathogen Streptococcus pyogenes and other bacteria. She published the finding in 2011 in Nature. In the same year, she initiated a collaboration with Jennifer Doudna. Together, they showed how the bacterial protein Cas9 led by two guide RNAs (crRNA and tracrRNA) can identify targets in invading genes. They also showed how the system can be readily reprogrammed to be applied on any gene - which has proven to be a very versatile gene editing tool. This work was published 2012 in Science.

Make it or break it: how bacteria balance production and degradation of the ‘magic spot’ signaling alarmone

Details: Created: Monday, 11 May 2020 15:36

Picture Rel [2020-05-11] When stressed or starved, bacteria regulate their metabolism by producing signalling molecules called alarmones or ‘magic spots’. In the majority of bacteria, the magic spot compounds are both made and destroyed by a large, complex enzyme called Rel. The question of how Rel switches from making the alarmone to degrading it was finally resolved by an international team from Sweden – Vasili Hauryliuk (MIMS & UCMR) – and Belgium: Jelle Hendrix (Hasselt University) and Abel Garcia-Pino (Université Libre de Bruxelles). The results of this study were published in the high impact journal Nature Chemical Biology ("A nucleotide-switch mechanism mediates opposing catalytic activities of Rel enzymes", 11 May 2020).

The team have studied a Rel enzyme from a thermophilic bacterium Thermusthermophilus using a combination of structural (X-ray), biochemical (enzymology) and biophysical (single molecule FRET assays and Isothermal Titration Calorimetry). Since the T.thermophilus has an optimal growth temperature of about 65 °C, by solving the structures at room temperature the researchers could slow down the enzyme enough to ‘catch’ it in the act of synthesising or degrading the alarmone. It turned out that binding of the substrates to the active site region (domain) that is responsible for synthesis of the ‘magic spot’ allosterically inhibits the domain responsible for its degradation – and vice versa, binding of the substrates to the degradation domain inhibits the synthesis domain. This simple but elegant mechanism ensures that bacteria avoid wasteful production and degradation of the magic spot signalling molecule. Biochemical characterisation of T.thermophilus was performed in Umeå by Dr. Hiraku Takada who is supported by a personal postdoctoral fellowship from the Umeå Centre for Microbial Research (UCMR).

Bacteria use small molecules to slam the brakes on their own growth

Details: Created: Wednesday, 29 April 2020 11:29

[2020-04-29] An international research team under the lead of scientists at the Umeå Center for Microbial Research (UCMR) and The Laboratory for Molecular Infection Medicine Sweden (MIMS) have uncovered a new kind of regulatory system of toxin and antitoxin proteins in bacteria that could be a defense system against viral attack. The bioinformatic identification of the proteins and their experimental validation are now published in the high impact journal Proceedings of the National Academy of Sciences of the US (PNAS, 28 April 2020)

When bacteria get stressed e.g. through antibiotic treatment or the lack of nutrients, they slow down their growth mechanism by small signaling molecules called Alarmones. The Atkinson and Hauryliuk labs at Umeå University have worked on the proteins that make and degrade alarmones for over a decade. They previously revealed the ubiquitous presence of small proteins that make alarmones, called small alarmone synthetases or SASs, encoded in bacterial genomes.

It was an unanswered question why bacteria carry SAS proteins in addition to their standard tool-set for alarmone synthesis and degradation. Now, Gemma C. Atkinson, Vasili Hauryliuk and their colleagues found an explanation. They showed that some SASs are components of so-called toxin-antitoxin (TA) systems.

Toxin-antitoxins genes are enigmatic components of microbial genomes. What toxins of TA systems all have in common is that they slam the brakes on growth and reproduction. This is counteracted by their antitoxins which are encoded by adjacent genes. Antitoxins can also work in different ways, either binding to the toxin to stop its action, or counteracting the effect of the toxin in an indirect way.

Immune testing for Coronavirus created by researchers in Västerbotten

Details: Created: Tuesday, 21 April 2020 16:54

[2020-04-15] Researchers at Umeå University and Norrland University Hospital have developed an antibody test for the new Corona virus

People who were once infected with the coronavirus also become immune to re-infection. By using tests that measure whether the body's immune system has reacted to the coronavirus, it is possible to identify people who are resistant to the infection. This is of particular importance for staff working in healthcare or working with risk groups, but also to determine so-called flock immunity, when enough people are immune to the spread of the virus.

On initiative of University Lecturer Mattias Forsell and through collaboration between researchers at Umeå University and the University Hospital in Umeå, a test has been developed in a short time, which could show immunity to coronavirus.

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