Martin Hällberg's Group
Structural basis of RNA biogenesis
We want to understand, on a molecular level, how proteins and RNA recognize each other and how their interaction interface mediates specificity. To this end we study both apo-structures and RNA co-crystal structures of proteins involved in processing and modification of RNA. Most transcripts undergo processing and modification. Out of these, transfer RNA is by far the most studied and modification of tRNA has been the focus of our lab for several years. Recently, we have expanded into structural studies on the general process of mitochondrial RNA biogenesis: transcription, processing and modification.
|Martin Hällberg||Senior researcher|
|Patrick Scicluna||PhD student, Graduate Student|
|Saba Shahzad||PhD student, Graduate Student|
|Sagar Sridhara||PhD student, Graduate Student|
Structure of mitochondrial poly(A) RNA polymerase reveals the structural basis for dimerization, ATP selectivity and the SPAX4 disease phenotype.
Nucleic Acids Res. 2015 Oct;43(18):9065-75
Structure of the nuclease subunit of human mitochondrial RNase P.
Nucleic Acids Res. 2015 Jun;43(11):5664-72
TEFM is a potent stimulator of mitochondrial transcription elongation in vitro.
Nucleic Acids Res. 2015 Mar;43(5):2615-24
Making proteins in the powerhouse.
Cell Metab. 2014 Aug;20(2):226-40
Structure of the human MTERF4-NSUN4 protein complex that regulates mitochondrial ribosome biogenesis.
Proc. Natl. Acad. Sci. U.S.A. 2012 Sep;109(38):15253-8