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.
An unexpected finding from Julian Sale’s group in the LMB’s PNAC Division has revealed that a specialised histone protein called H3.3 is needed for packaging UV-damaged DNA during replication. Use of this histone may act as a flag to help the cell find and repair the damage once replication has been completed, potentially reducing the chance of harmful mutations.
Every time a cell divides, the double-stranded DNA needs to be copied with the DNA strands separated in a replication fork.
Research from the LMB’s PNAC Division has revealed a new mechanism that cells use to fight infection. Jerry Tam and other members of Leo James’s group have discovered that the protein complement C3, which covalently labels viruses and bacteria in the bloodstream, activates a potent immune response upon cell invasion.
Molecular biologists chemically modify proteins to label them for easy identification.
New research from Madan Babu’s group in the LMB’s Structural Studies Division, in collaboration with Toby Gibson from the European Molecular Biology Laboratory in Heidelberg, has shown that the targeted movement of mRNA molecules to allow proteins to be synthesised in specific locations has important implications in cell signalling and development.
Whilst a mother’s metabolism provides essential nutrients to enable embryonic development, both mother and embryo can also produce reactive metabolites that can damage DNA. Research undertaken by Nina Oberbeck in KJ Patel’s group, in the LMB’s PNAC Division, has uncovered how the embryo is protected from these genotoxins.
Birth defects are common and are a substantial burden to human health, but their causes are complex and often due to many factors.
Research carried out by Anne Bertolotti’s group in the LMB’s Neurobiology Division has identified a novel protein, named Adc17, that acts as an inducible chaperone to help cells make more proteasome when needed.
Cells and organisms constantly need to adapt to maintain protein homeostasis under adverse stress conditions in order to avoid cell death. Cells have evolved numerous and sophisticated protein quality control systems to adapt to changes in their environment.
The latest advances in cryo-electron microscopy have enabled Sjors Scheres’ group, from the LMB’s Structural Studies Division, together with collaborators from Beijing in China, to solve the structure of human gamma-secretase, a membrane protein complex that has an important role in Alzheimer’s disease.
Gamma-secretase is made up of four different proteins which are all embedded within the cell membrane.