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  • Labeling proteins with ubiquitin paves new road to cell regulation research

    Human cells have a sophisticated regulatory system that consists of labeling proteins with the 

    small molecule ubiquitin. In a first, a team from the Technical University of Munich (TUM) has 

    succeeded in marking proteins with ubiquitin in a targeted manner in test tubes as well as in 

    living  cells.  The  procedure  opens  the  door  to  exploring the inner workings of this vital 

    regulatory system.

    Plants, fungi, animals and humans express the protein ubiquitin. It comprises a sequence of 

    76 amino acids, making it a relatively small biomolecule. But its influence is far-reaching: the 

    type, position and number of ubiquitin molecules bound to proteins determine their stability, 

    function, and location within the cell.


    "Virtually every process in the cell is directly or indirectly affected by ubiquitin. That is why 

    malfunctions of this labeling mechanism are associated with the development and progress

    ion of cancer and many other severe diseases," explains Kathrin Lang, Professor of Synthetic 

    Biochemistry at the Technical University of Munich.


    The discovery of the important role this cellular regulatory system plays in the controlled 

    degradation of proteins was acknowledged with the 2004 Nobel Prize in Chemistry. But, in 

    many cases the details of how ubiquitin modifications affect the function of cells remains 

    unclear. Kathrin Lang's team has now developed a method for attaching ubiquitin labels to 

    targeted proteins—a key to exploring the system.


    A bacterial enzyme creates new compounds


    Lang's team uses two tricks to circumvent the complicated natural system: They incorporate a 

    novel modified amino acid, at which the bacteria-derived enzyme sortase can attach ubiquitin 

    or a ubiquitin-similar molecule.

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