Max Planck Laboratory
Max Planck Research Group Leader
Dr. Sebastian Glatt
T +48 12 664 6322
F +48 12 664 6902
MCB, Gronostajowa 7a str
Max Planck Group
Molecular mechanisms of translational control
Research in the Glatt group combines structural biology (x-ray crystallography and electron microscopy), molecular biology, protein biochemistry, biophysics, and cell biology to understand specific regulatory mechanisms of protein synthesis.
We study different translation control mechanisms, which regulate the production of specific sets of proteins by chemical modifications of tRNA molecules. Every protein in the cell is produced by the ribosome, which uses transfer RNA (tRNA) molecules to translate the sequence information coded in mRNAs into correctly assembled poly-peptide chains. The decoding/translation of genetic information is based on the recognition of a respective codon by its corresponding tRNA anticodon triplet.
The lab is focusing on understanding the molecular mechanisms that lead to the specific base modifications in anticodons of tRNAs. These modifications have a strong influence on the efficiency and accuracy of the codon-anticodon pairing and therefore regulate the translational rates and folding dynamics of protein synthesis. Recent findings have shown that alterations of these modification pathways play important roles in the onset of certain neurodegenerative diseases and cancer.
Crystal structures of DmcElp3 (Glatt et al., NSMB 2016), the Elp456 subcomplex (Glatt et al., NSMB 2012) and the Kti11/Kti13 heterodimer (Glatt et al., Structure 2015)
Future projects and goals
Using structural biology we would like obtain individual snapshots of the underlying modification reactions and their regulatory signaling cascades. In addition, we would like to establish suitable cellular disease models that will allow us to specifically test structure guided mutations for their role in neurodegenerative diseases. In addition, we would like to further understand the link between the respective modification reactions, metabolic pathways and the onset of certain diseases.
· EMBO Installation Grant 2015-2018
· NCN OPUS10 NZ 2016-2019
· NCN POLONEZ1 (Monika Gaik) 2016-2018
· FNP FirstTEAM 2016-2019
· FNP Homing (Ting-Yu Lin) 2017 – 2019
We are always seeking for interested and highly motivated Master, PhD or Postdoc candidates. Please contact us for further details (sebastian.glatt[a.t]uj.edu.pl).
- Dauden MI, Kosinski J, Kolaj-Robin O, Desfosses A, Ori A, Faux C, Hoffmann NA, Onuma OF, Breunig KD, Beck M, Sachse C, Seraphin B, Glatt S*, Müller CW*; Architecture of the yeast Elongator complex, EMBO Rep. 2017 Feb;18(2)
- Glatt S, Zabel R, Kolaj-Robin O, Onuma OF, Baudin F, Graziadei A, Taverniti V, Lin TY, Baymann F, Séraphin B, Breunig KD, Müller CW; Structural basis for tRNA modification by Elp3 from Dehalococcoides mccartyi, Nat Struct Mol Biol. 2016 Sep;23(9)
- Glatt S, Zabel R, Vonkova I, Kumar A, Netz D, Pierik A, Lill R, Gavin AC, Balbach J, Breunig KD, Müller CW; Structure of the Kti11/Kti13 Heterodimer and Its Double Role in Modifications of tRNA and Eukaryotic Elongation Factor 2; Structure 2015 Jan 6;23(1)
- Glatt S, Müller CW; Structural insights into Elongator function; Curr Opin Struct Biol. 2013 Apr;23(2)
- Glatt S, Séraphin B, Müller CW; Elongator: transcriptional or translational regulator? Transcription. 2012 Aug 14;3(6)
- Glatt S, Létoquart J, Faux C, Taylor N, Séraphin B and Müller CW; The Elongator subcomplex Elp456 is a hexameric RecA-like ATPase; Nat Struct Mol Biol. 2012 Feb 19;19(3)