Thousands of Protein Interactions Identified
News Oct 05, 2015
Until now, this had only been possible when a small number of proteins were brought together in an artificial setting. “We are now able to see which proteins work together and where they are linked”, explains Utrecht University Prof. Albert Heck. “This is essential in order to understand how proteins operate in a cell under healthy conditions, and what goes wrong in diseases.”
The millions of proteins in our cells conduct all of the processes that regulate life, in constantly shifting interactions. These interactions are a lively dynamic of links between proteins - often numbering in the hundreds. Until recently, pharmaceuticals inhibited a single protein, but it is more effective to treat diseases by sabotaging the interactions between proteins. This is because the protein inhibited may actually have another useful, or even vital function in a healthy cell, which often results in undesirable side effects during treatment.
Identifying all of the links at a single glance
The technique for identifying the cooperation between proteins is called ‘cross-linking mass spectrometry’. This technique has been available for some time, but until now it could only make these interactions visible if a small number of purified proteins were placed together in a small container. However, only a limited amount of information can be derived in such an artificial setting. But now, thanks to improvements in mass spectrometry sequence analysis and a new search algorithm, researchers can study all of the links between all of the proteins present in a cell at a single glance.
From dozens to thousands
“We’ve managed to identify around 2,100 of these links, while before we were only able to map out tens or hundreds”, according to Albert Heck, Professor of Biomolecular Mass Spectrometry and Proteomics at Utrecht University. “For example, we have identified more than 100 links in the ribosome, the machine that is responsible for protein synthesis in the cell. Plus, we’ve been able to differentiate between the partners that collaborate with one another all the time from those with more superficial partnerships in this protein complex.”
Synthetic DNA Shuffling Enzyme Outpaces Natural CounterpartNews
A new synthetic enzyme, crafted from DNA rather than protein, flips lipid molecules within the cell membrane, triggering a signal pathway that could be harnessed to induce cell death in cancer cells. Researchers say their lipid-scrambling DNA enzyme is the first in its class to outperform naturally occurring enzymes – and does so by three orders of magnitudeREAD MORE
Eating Activates Calorie-Burning FatNews
The importance of the human brown adipose tissue (BAT) has become clearer during the past ten years. Coldness is one of the most effective activators of the BAT metabolic function but, in rodents, eating has also been shown to activate BAT. The debate on whether eating has the same effect on humans has lasted for decades. Now, the researchers at Turku PET Centre have proven that having a meal increases oxygen consumption in human BAT to the same extent as coldness.READ MORE
Penn Medicine Biochemist Receives Major Award for Research on Epigenetic Protein Modifications via Mass SpecNews
Benjamin A.Garcia, PhD, an expert in quantitative proteomics and Presidential Professor of Biochemistry and Biophysics in the Perelman School of Medicine at the University of Pennsylvania, has been awarded the Biemann Medal by the American Society for Mass Spectrometry (ASMS). The early-career award recognizes significant achievement in basic or applied mass spectrometry.