Danish researchers reveal how the MRSA bacterium handles stress



News

An international team of researchers has revealed a fundamental mechanism responsible for handling stress in staphylococci when they are exposed to antibiotics. Figure: Ditlev E. Brodersen.

2018.01.15 | Research

Danish researchers reveal how the MRSA bacterium handles stress

An international team of researchers has revealed a fundamental mechanism responsible for handling stress in staphylococci when they are exposed to antibiotics. It is expected that the research results eventually can be used to develop new antibiotics that circumvent such stress mechanisms.

Dual Roles of ZC3H18 in Nuclear RNA Metabolism. Schematic representation of the dual engagement of ZC3H18 in RNA transcription and decay processes.  Left: ZC3H18 interacts with the CBCA complex (CBC and the ARS2 protein) to regulate protein-coding gene transcription directly or indirectly. The question mark indicates the elusive role of the histone-interacting domain and its modification in facilitating ZC3H18 function.  Right: Short non-coding RNAs, exemplified here by 3’extended snRNAs, are targeted by ZC3H18 in a process requiring interaction with both the CBCA and NEXT complexes. Such RNA decay can also occur ZC3H18-independently via direct NEXT exosome targeting. C, CBCA-interacting domain; H, histone-interacting domain; N, NEXT-interacting domain.

2018.01.03 | Research

Researchers reveal dual role for human RNA decay factor

Researchers at Aarhus University have characterized the human RNA decay factor ZC3H18 and discovered its unanticipated role in the production of protein-coding RNA. The new study, published this week in Cell Reports, therefore reveals a double-faced activity of ZC3H18 in nuclear RNA fate decisions.

Figure caption: Left: Unsharpened (transparent light blue) and sharpened (solid) cryo-EM density maps of human TRPM4 in nanodiscs as viewed from the side. The ion channel is composed by four domains which are colored in each their solid color. Middle: Ribbon diagram of human TRPM4. A calcium binding site belonging to one of the monomers is marked with a box. Right: A zoom-in on the calcium binding site with the coordinating residues represented by sticks and their helices in ribbons. The ribbon diagram is overlaid with the densities of the calcium structure (gray mesh) and the difference density (blue mesh) between the calcium-bound structure and the calcium-free structure. Figure: Henriette Autzen.
Henriette Elisabeth Autzen, who is employed as a postdoc at the Department of Molecular Biology and Genetics at Aarhus University in Denmark, is stationed at the University of California, San Francisco, USA, where she and her American colleagues have published their determination of two structures of the human calcium-activated cation channel, TRPM4, in <em>Science</em>. Photo: University of California, San Francisco.

2017.12.15 | Research

A Channel in the Heart of the Matter

How cells control the movement of ions, electrically charged species, in and out of the cell is a grand puzzle, whose completion will allow a thorough fundamental understanding of human physiology. A Danish-American team of researchers has found a piece of the puzzle with their determination of two structures of the human calcium-activated cation…

Bill Gates (on the right side of the table, in the middle) listening to the researcher’s plans for their research. The head of the project from Aarhus University, Professor Jens Stougaard, is seen on the left side of the table, 2nd from the left. Photo: ©Bill & Melinda Gates Foundation/Alain Brin.

2017.12.11 | Research

Bill Gates met with researchers from Aarhus University

Bill Gates recently met with researchers from the Department of Molecular Biology and Genetics at Aarhus University to discuss the sustainable use of biological nitrogen fixation that allows legumes to use atmospheric dinitrogen as a nitrogen source.

Events

Tue 16 Jan
13:00-15:00 | Nobel Auditorium, Building 1482–105 i Nobelparken
Information meeting about the calls from "Innovationsfonden" 2018
At the meeting you will be able to hear about the foundation's support schemes and receive the latest news about the proposals in 2018. There will also be an opportunity to ask questions to representatives from the Innovation Fund. The meeting is in English. Registration is not required. From 13-14:
Fri 26 Jan
13:00-15:00 | 1170-347, Ole Worms Allé 3
Qualifying exam: Joachim Vilstrup: Structural and Biochemical Studies of Human PCSK9 and SORCS2
Joachim Vilstrup
Fri 26 Jan
13:15-15:15 | Building 1593, room 012, the Lecture Theatre, iNANO House
PhD defence: Henriette Kristina Søster Frislev: Usability of cytotoxic protein-fat complexes
Henriette Kristina Søster Frislev

PhD defences

Henriette Kristina Søster Frislev

2018.01.26 | Talent development

Henriette Kristina Søster Frislev: Usability of cytotoxic protein-fat complexes

PhD defence, Friday, 26 January 2018. Henriette Kristina Søster Frislev

Jeryl Cheng

2018.01.18 | Talent development

Jeryl Cheng: The role of LysM Receptor-like kinases in Lotus japonicus: Are you my Friend or Foe?

PhD defence, Thursday 18 January 2018. Jeryl Cheng.