Seminar: Prof. Henning D. Mootz

Chemical approaches to study and control protein function: Protein splicing and ubiquitin/SUMO

Date:
17 June 2014 00:00 hrs.
Location:
Figdor Lecture Theatre, 8th floor RIMLS Building, Geert Grooteplein 26-28, route 289
Title:
Chemical approaches to study and control protein function: Protein splicing and ubiquitin/SUMO
Speaker(s):

Prof. Henning D. Mootz, Institute for Biochemistry, University of Münster, Germany

Host(s):

Prof. Roland Brock, Dept. of Biochemistry, Radboudumc

17-06-2014 00:00:00Europe/AmsterdamChemical approaches to study and control protein function: Protein splicing and ubiquitin/SUMO  Figdor Lecture Theatre, 8th floor RIMLS Building, Geert Grooteplein 26-28, route 289Rimlsrimls@radboudumc.nl

Remarks / more information:

Mootz , HenningPosttranslational modification is a powerful strategy employed by Nature to diversify the chemical structure of proteins and thereby modulate their function. Likewise, the artificial chemical modification of proteins is important for many applications, for example to enable biophysical studies with suitable probes or to create antibody drug conjugates as designer protein therapeutics. 

I will highlight our research efforts in the fields of protein splicing and ubiquitin-like modifiers. Protein splicing by inteins can be exploited in several ways to introduce synthetic components into proteins, both in the test tube and on/in live cells. We have identified and engineered several inteins to facilitate this approach. Ubiquitylation and SUMOylation are affecting a myriad of proteins, yet the precise molecular consequences are often difficult to study, because the protein conjugates under investigation cannot be obtained in defined and homogeneous form by enzymatic means. We have developed a chemical conjugation approach to such conjugates based on click chemistry that circumvents these problems.

Key Publications:

  • Photocontrol of protein activity mediated by the cleavage reaction of a split intein, Angew. Chem. Int. Ed., 50, 3249-3252, 2011.
  • Expanded Click Conjugation of Recombinant Proteins with Ubiquitin-Like Modifiers Reveals Altered Substrate Preference of SUMO2-modified Ubc9, Angew. Chem. Int. Ed., 50: 9888-9892, 2011.
  • An atypical naturally split intein engineered for highly efficient protein labeling, Angew. Chem. Int. Ed., 53: 1306-1310, 2014.

 



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