MRC Laboratory of Molecular Biology
One of the world's leading research institutes, our scientists are working to advance understanding of biological processes at the molecular level - providing the knowledge needed to solve key problems in human health.
Protein phosphorylation is a key post-translational modification that is used to regulate many essential cell processes. A phosphate group is added to a specific site in a protein to switch that protein on or off, depending on its role. It has been challenging to understand the function of protein phosphorylation because it is difficult to make phosphorylated proteins. However, a new method developed by Jason Chin’s group in the LMB’s PNAC Division could revolutionise this research.
Small molecules are often used to regulate the functions of proteins and provide many drugs and tools for understanding biological pathways. However, selectively controlling a specific target protein within living cells is a major challenge. Jason Chin’s group from the LMB’s PNAC Division have created a new technique called BOLT that can selectively regulate specific proteins inside cells that could not previously be targeted.
There is compelling evidence that in the distant past, our single-celled ancestors used RNA, a chemical cousin of DNA, for both genetic information storage and metabolism. This primordial “RNA world” would have needed an RNA enzyme able to replicate itself and other primordial “RNA genes”.
The structure of the actin-like protein ParM in different states has been revealed by Tanmay Bharat and Jan Löwe in collaboration with Garib Murshudov from the LMB and Carsten Sachse from the EMBL. Using electron cryo-microscopy (cryo-EM) they determined the structure of ParM to almost atomic resolution and revealed how this protein carries out the process of plasmid DNA segregation in growing bacterial cells.
In their latest research on the DNA replication machinery from Mycobacterium tuberculosis, Ulla Lang in Meindert Lamers’ group in the LMB’s Structural Studies Division and collaborators at the Harvard School of Public Health in Boston, have revealed the existence of a novel exonuclease that proofreads new DNA as it is synthesised. This newly discovered proofreader prevents mutations in the bacterium and could be a successful drug target.
The existence of an endogenous daily clock in humans is well known: it is what drives the 24-hour sleep/wake rhythm to match the daily cycle of night and day. That this biological circadian rhythm occurs in individual cells, and that they continue to ‘tick’ in a petri dish is now well-accepted scientifically, but the mechanism that allows cellular clocks to keep time remains poorly understood.