Science for Health
07 November 2012
The MRC has awarded NIMR a sum of money under its MRC Centenary Early Career Awards scheme, to help support early career researchers.
NIMR staff were invited to apply for MRC Centenary Early Career Awards in four categories: Programme Leader Track, postdoctoral scientists, late stage PhD students, and training/travel grants. The awards were made to encourage interdisciplinary and innovative science, and to enable staff to gain access to, or training in, new technology. An internal review panel at NIMR considered the applications and has made 46 awards, highlighting the ‘best of group’ in each category.
Six awards were made:
Every cell in our body contains thousands of proteins that work as tiny machines to allow a cell to do its job. To work correctly, each protein must be in the right place at the right time. To help understand how this happens we have developed a new technology that allows us to rapidly fuse one protein to every other protein in the cell and score the resulting effects upon growth. This method gives us a glimpse into where proteins work in the cell and how we can modulate cellular activities by changing their location.
Nine awards were made:
Protein phosphorylation is a well-characterised mechanism through which information is transmitted in a cellular environment. The enzymatic addition or removal of phosphate groups can act as a switch. In many cases, the addition of a phosphate to a protein creates a binding surface to which other proteins can be recruited. In the response to DNA damage, such a mechanism enables the recruitment of DNA repair machinery. The protein kinases that are activated in the response to DNA damage are called PIKKs. Disruption of the interaction between phosphorylated PIKK accessory protein, Tel2, and a novel phospho-reader protein leads to a dramatic decrease of cellular PIKK concentrations. My project will describe these interactions at the atomic level.
Nine awards were made.
In cells the production of protein occurs via two steps. First, genes in the DNA are transcribed into an RNA message (mRNA) by a cellular ‘machine’ called RNA polymerase (RNAP). Then, this RNA code is translated into a protein by a second machinery called the ribosome, which is made by both proteins and RNAs. In each cell the activity of RNAP needs to be precisely regulated to produce the right RNAs and proteins at the right time. Working with the group of Prof. Finn Werner at UCL we will use the Archaea RNAP model system to investigate how the NusA and NusE/NusG proteins recognize the target RNA sequences in a specific fashion and regulate the synthesis of ribosomal RNA.
The immune system employs many ways to combat infection. One is to produce antibodies - proteins produced by white blood cells known as B cells - which can identify and neutralise foreign material. We found a spontaneous genetic mutation that leads to a severe impairment in the development of B cells and a defect in the production of antibodies. I plan to identify the gene that is affected by this mutation and characterise its impact on the immune system. This research will contribute to our basic understanding of how B cells function and how the immune system makes antibodies to combat infection.
22 awards were made.
The 100 years, 100 scientists, 100 schools project aims to celebrate the centenary of the MRC by giving 100 NIMR scientists the opportunity to interact with local school children and really make a difference to how they perceive science. Many scientists were inspired as children by meeting, or seeing on TV, someone who demonstrated just how exciting science can be. This project aims to encourage NIMR scientists to be that inspiring person for the next generation.
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