Researchers at the LMB have solved the elusive 3D structure of activated Parkin, an enzyme implicated in early-onset Parkinson’s disease. Led by David Komander’s group in the LMB’s PNAC Division, in collaboration with the LMB’s Biological Mass Spectrometry facility, this new work reveals insights into previously unstudied parts of this important protein and helps explain why families with certain mutations in Parkin suffer from early-onset Parkinson’s disease.
Work by Joe Yeeles’ group in the LMB’s PNAC Division has for the first time revealed the earliest responses when the eukaryotic DNA replication machinery, the replisome, collides with DNA damage.
Every time a cell divides, its DNA must be replicated so that each daughter cell inherits a complete copy of the genome.
Scientists in Leo James’ group in the LMB’s PNAC Division, in collaboration with Till Böcking’s group at the University of New South Wales, Australia and Adolfo Saiardi’s group at the MRC Laboratory for Molecular Cell Biology, have uncovered how the HIV virus stabilises its capsid by binding to an abundant cellular polyanion, IP6.
In our day-to-day lives we execute spatially targeted movements with ease and seemingly without much thought. These movements may include reaching for your morning cup of coffee, checking your mirrors on your drive into work, or catching a cricket ball.
Scientists in Philipp Holliger’s group in the LMB’s PNAC Division have created a new type of genetic replication system to demonstrate how the first life on Earth – in the form of RNA – could have replicated itself.
Our understanding of life’s early history is limited but a popular theory for the earliest stages of life on Earth is that it was founded on strands of RNA, a chemical cousin of DNA.
Work from Madan Babu’s group in the LMB’s Structural Studies Division, spearheaded by Charles Ravarani and in collaboration with Alexandre Erkine’s group at Butler University, has for the first time harnessed next generation sequencing and machine learning to develop a high throughput screen to uncover disordered regions of proteins that are functional within cells.
Proteins, the molecular machines of the cell, are formed from chains of amino acids.
During a viral infection, our immune system produces potent antiviral molecules which are hugely important for restoring us to health. However, if made at the wrong time these molecules can be damaging, leading to autoimmune diseases such as rheumatoid arthritis and multiple sclerosis. Our antiviral response must therefore be tightly controlled so that we are protected against infection but do not suffer from autoimmune disease.
Ageing is characterised by a decline in function at both the cellular and organismal level and is the major risk factor for several neurodegenerative disorders, including Alzheimer’s and Parkinson’s disease. One of the key cellular processes that is affected during ageing is the transport system that nerve cells use to deliver components to different locations.
Cytoplasmic dynein-1, a protein that transports cargos along microtubule tracks throughout the cell, binds to dynactin and cargo adaptor proteins to carry its cargos over long distances. Various cargos use different adaptors to recruit dynein for transport. Until now, it has not been clear whether all cargos recruit dynein in the same way and how different cargo adaptors act.
Previous work from KJ Patel’s group in the LMB’s PNAC Division revealed that aldehydes – such as acetaldehyde, a by-product of alcohol metabolism – can damage our DNA. Further research by the group showed that our cells are protected against these toxic aldehydes using a two-tier protection system: enzymes that remove these aldehydes (tier-1) and DNA repair that fixes the damage they cause (tier-2).