Dr. Erzberger received his undergraduate degree in Biological Chemistry from Harvard University. He obtained his Ph.D. in the lab of James Berger at the University of California, Berkeley, studying DNA replication initiation in bacteria, with a particular focus on the universal bacterial initiator DnaA. He was able to address longstanding questions on the mechanism of origin firing by solving crystal structures of DnaA in both monomeric (ADP-bound) and oligomeric (ATP-bound) forms. In addition, he collaborated with the lab of Karsten Weis to understand the functional relationship between the DExD/H ATPase Dbp5 and components of the nuclear pore complex (NPC) in mRNA export, helping to establish a new paradigm for the function and regulation of the DEAD-box family of enzymes.

During his postdoctoral training in the laboratory of Nenad Ban at the ETH Zürich, Dr. Erzberger focused on studies of the eukaryotic translation initiation machinery, developing a novel hybrid structural approach, combining x-ray crystallography, cryo-electron microscopy and mass-spectrometry to investigate the role of eIF3, a large, multiprotein initiation factor. These studies provided a mechanistic framework for how eIF3 is able to coordinate the initiation process, guiding the recruitment, assembly and regulation of the translation initiation machinery.

Since joining the faculty of UT Southwestern in 2015, Dr. Erzberger has been implementing a similar hybrid structural approach to investigate the regulatory aspects of ribosome biogenesis, in particular the important links that connect ribosome synthesis and cellular growth.


Graduate School
Harvard College (1995), Biocchemical Sciences
Graduate School
Univ of California-Berkeley (2005), Molecular Biology

Research Interest

  • Structural and biochemical characterization of dynamic protein-RNA complexes during ribosome biogenesis


Featured Publications LegendFeatured Publications

Architecture of the large subunit of the mammalian mitochondrial ribosome.
Greber BJ, Boehringer D, Leitner A, Bieri P, Voigts-Hoffmann F, Erzberger JP, Leibundgut M, Aebersold R, Ban N Nature 2014 Jan 505 7484 515-9
Nucleotide and partner-protein control of bacterial replicative helicase structure and function.
Strycharska MS, Arias-Palomo E, Lyubimov AY, Erzberger JP, O'Shea VL, Bustamante CJ, Berger JM Mol. Cell 2013 Dec 52 6 844-54
Structure of the C-terminus of the mRNA export factor Dbp5 reveals the interaction surface for the ATPase activator Gle1.
Dossani ZY, Weirich CS, Erzberger JP, Berger JM, Weis K Proc. Natl. Acad. Sci. U.S.A. 2009 Sep 106 38 16251-6
Structural synergy and molecular crosstalk between bacterial helicase loaders and replication initiators.
Mott ML, Erzberger JP, Coons MM, Berger JM Cell 2008 Nov 135 4 623-34
The septin family of GTPases: architecture and dynamics.
Weirich CS, Erzberger JP, Barral Y Nat. Rev. Mol. Cell Biol. 2008 Jun 9 6 478-89
Structural basis for ATP-dependent DnaA assembly and replication-origin remodeling.
Erzberger JP, Mott ML, Berger JM Nat. Struct. Mol. Biol. 2006 Aug 13 8 676-83
Nucleotide-dependent conformational changes in the DnaA-like core of the origin recognition complex.
Clarey MG, Erzberger JP, Grob P, Leschziner AE, Berger JM, Nogales E, Botchan M Nat. Struct. Mol. Biol. 2006 Aug 13 8 684-90
Activation of the DExD/H-box protein Dbp5 by the nuclear-pore protein Gle1 and its coactivator InsP6 is required for mRNA export.
Weirich CS, Erzberger JP, Flick JS, Berger JM, Thorner J, Weis K Nat. Cell Biol. 2006 Jul 8 7 668-76