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Krypotou, E., Scortti, M., Grundström, C., Oelker, M., Luisi, B.F., Sauer-Eriksson, A.E. & Vázquez-Boland, J. Control of bacterial virulence through the peptide signature of the habitat. (2019) Cell Reports, 26, 1815-1827.
We identify a major control mechanism of Listeria virulence based on antagonistic regulation by environmental peptides.Activity levels of the virulence regulator PrfA depend on the net balance between the rates of synthesis of the PrfA-activating cofactor GSH from exogenous peptide-derived cysteine and of direct, promiscuous PrfA inhibition by non-cysteine-containing peptides
Professor Erik Johansson has published an article in Nature Communications named “Structural consequence of the most frequently recurring cancer-associated substitution in DNA polymerase epsilon“. The study was a collaboration with Uppsala University and University of Nebraska Medical Center. The article can be found at: “www.nature.com/articles/s41467-018-08114-9”
Magnus Wolf-Watz was named professor in biophysical chemistry on May 1:st 2018.
Ronnie Berntsson has be awarded the Swedish Foundation Starting grant for research on Type 4 Secretion Systems.
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The Swedish Research Council has decided to award a 25.2 MSEK grant to a coalition of research groups at Umeå University and the University of Helsinki within the call “Research environment grant within infection and antibiotics”.
The project “Multimodal imaging and proteomics to study flavivirus replication and molecular disease mechanisms” is headed by flavivirologist Anna Överby Wernstedt at Umeå University and includes the biostruct-affiliated group of Lars-Anders Carlson. The other two teams involved in the collaboration are the Umeå-based group of Richard Lundmark and the Helsinki-based group of Sarah Butcher.
As of 1st of December Ronnie Berntsson has started as a Wallenberg Molecular Medicine Fellow at Umeå University.
This paper from the Wolf-Watz lab describes the discovery of a fundamentally new mechanism underlying protein-protein interactions. The chaperone-binding domain of the Yersinia effector protein YopH was found to lose its globular structure upon formation of a wrap-around architecture with its chaperone SycH. The mechanism is best described as a coupled binding and disordering event. The finding was enabled by an integrated structural biology approach by a five-lab effort and centered on NMR, SAXS and computational chemistry.
The article is published in Journal of Molecular Biology (2018), 430, 3157.
On June 1st Artur Dingeldein successfully defended his PhD thesis.