J. Preben Morth did his M.Sc at Aarhus University with Asc. Prof. Morten Kjeldgaard. Investigating the complex between the eukaryotic translational release factors eRF1 and eRF3. In 2001 he continued his career at the European Molecular Biology Laboratory (EMBL) in Hamburg were he was accepted into the international PhD program. Together with his supervisor Dr. Paul A Tucker he investigated two-components systems from Mycobacterium tuberculosis (MtB). They took a systems biology approach, to identify and functionally link the sensor histidine kinase (Rv3220c) to the response regulator (Rv1626). He cloned and purified the candidate genes and established a biochemical link using an in vitro phosphorylation assay. This was the first transcriptional antitermination system identified which follows an activation scheme, otherwise only found for the two-component systems. Two-component systems are often associated with transcriptional control through DNA binding, while the antitermination systems are RNA binding. They named the factors in the system “phosphorylation dependent transcriptional antitermination regulator/sensor”, PdtaR and PdtaS (4,5).
J. Preben Morth moved back to Aarhus in 2005 as a postdoc in the group of Prof. Poul Nissen to investigate the structure of the Na+,K+-ATPase, the key membrane bound enzyme involved with maintaining the sodium and potassium gradient across the plasma membrane in most mammalian cell. The Na+,K+-ATPase is hetero trimeric membrane complex with an alpha, beta and gamma subunit, the complete structure was determined to 3.5 Å, revealed the molecular composition and the interaction between each of the subunits. Structural interpretation revealed a novel regulatory element that was assigned to the C-terminal region (1). From 2008-2010 He advanced from assistant professor to asc. professor at Aarhus University before accepting a position at NCMM.
The Morth laboratory focus pursue a structural systems biology approach to on anion transporters involved in the acid/base homeostasis.
1. Laursen M, Bublitz M, Moncoq K, Olesen C, Young H, Moller JV, Nissen P, Morth JP (2009)
“The structure of sarceplasmic reticulum Ca2+-ATPase bound to cyclopiazonic acid reveals a complexed divalent ion” J Biol Chem. 284,13513-8
2. Morth J. P., Poulsen H., Toustrup-Jensen M. S., Schack V. R., Egebjerg J., Andersen J. P., Vilsen B. & Nissen P. (2009) The structure of the Na+,K+-ATPase and mapping of isoform differences and disease-related mutations. Philos. Trans. R. Soc. Lond. B. Biol. Sci, 364,1514, 217-27
3. Morth J. P., Pedersen B. P., Toustrup-Jensen M. S., Sorensen T. L., Petersen J., Andersen J.P., Vilsen B. & Nissen P. (2007) Crystal structure of the sodium-potassium pump. Nature 450, 1043-1049
4. Morth JP, Gosmann S, Nowak E, & Tucker PA (2005) A novel two-component system found in Mycobacterium tuberculosis. FEBS Lett 579: 4145-4148.
5. Morth JP, Feng V, Perry LJ, Svergun DI, & Tucker PA (2004) The crystal and solution structure of a putative transcriptional antiterminator from Mycobacterium tuberculosis. Structure 12: 1595-1605