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.
Structure of mitochondrial poly(A) RNA polymerase reveals the structural basis for dimerization, ATP selectivity and the SPAX4 disease phenotype.
Lapkouski M, Hällberg BM
Nucleic Acids Res. 2015 Oct;43(18):9065-75
Structure of the nuclease subunit of human mitochondrial RNase P.
Reinhard L, Sridhara S, Hällberg BM
Nucleic Acids Res. 2015 Jun;43(11):5664-72
TEFM is a potent stimulator of mitochondrial transcription elongation in vitro.
Posse V, Shahzad S, Falkenberg M, Hällberg BM, Gustafsson CM
Nucleic Acids Res. 2015 Mar;43(5):2615-24
Making proteins in the powerhouse.
Hällberg BM, Larsson NG
Cell Metab. 2014 Aug;20(2):226-40
Structure of the human MTERF4-NSUN4 protein complex that regulates mitochondrial ribosome biogenesis.
Spåhr H, Habermann B, Gustafsson CM, Larsson NG, Hallberg BM
Proc. Natl. Acad. Sci. U.S.A. 2012 Sep;109(38):15253-8