Trim-Away directly and rapidly destroys a fluorescent protein in an egg cell. From left: cell before introduction of antibodies directed against the protein and 10, 30, and 60 minutes thereafter. Dean Clift / MRC Laboratory of Molecular Biology

In our body, proteins carry out almost all essential processes, and protein malfunction causes many diseases. To study the function of a protein, researchers remove it from the cell and subsequently analyze the consequences. The two methods typically used are genome editing by CRISPR/Cas, and RNA interference, acting on the level of DNA or RNA, respectively. However, their influence on protein amounts is indirect and takes time. Scientists now present a new method, called Trim-Away, allowing to directly and quickly deplete any protein from any cell type. As Trim-Away can distinguish between different variants of a protein, it also opens up new venues for the therapy of diseases.

CRISPR-UMI relies on the addition of a high complexity barcoding system – or Unique Molecular Identifier (UMI) – that marks each single mutant clone and allows its tracking within a population. (c) Philipp Zaufel, maximcapra.com

CRISPR-UMI, a novel method developed at IMBA, facilitates extremely robust and sensitive screens by tracking single mutants within a population of cells. “The whole is greater than the sum of its parts” is an adage that applies to many concepts in biology. For genetic screens, however, it is the individual parts, i.e. the individual cells, that are the focus of the next generation of CRISPR-Cas9 screens. Single mutants within a population reveal new findings that could revolutionise target discovery and offer fresh insights into the biological systems of cell differentiation and cancer.

An aim of the project eTRANSAFE is to analyze whether and to what extent preclinical data enable reliable prediction of clinical findings. Felix Schmitt, Fraunhofer ITEM

(Hannover/Germany) The 40 million euro European project eTRANSAFE, to be kicked off at the end of September 2017, is aimed at speeding up the development of better and safer medicines for patients. Coordinated by the Fundació Institut Mar d'Investigacions Mèdiques (IMIM) and led by the pharmaceutical company Novartis, the project consortium is a public-private partnership of eight academic institutions, six SMEs, and twelve pharmaceutical companies. One of the project partners is Fraunhofer ITEM.

This image depicts a rendering of a cryo-electron tomogram of a Chlamydomonas pyrenoid, with tubule membranes (green and yellow) awash in a “sea” of Rubisco enzymes (blue). © ScienceDirect

Plants and algae use the enzyme Rubisco to fix carbon dioxide, removing it from the atmosphere and converting it into biomass. Algae have figured out a way to increase the efficiency of carbon fixation. They gather most of their Rubisco into a ball-shaped microcompartment called the pyrenoid, which they flood with a high local concentration of carbon dioxide. A team of scientists at Princeton University, the Carnegie Institution for Science, Stanford University and the Max Plank Institute of Biochemistry have unravelled the mysteries of how the pyrenoid is assembled. These insights can help to engineer crops that remove more carbon dioxide from the atmosphere while producing more food.

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