Department of Cell and Molecular Biology
Faculty, Graduate Program
Howard Hughes Medical Institute (HHMI) - Faculty Scholar
Ribosomes are large macromolecular machines that catalyze protein synthesis in all cells. In eukaryotic cells ribosome assembly requires a macromolecular machinery of >170 proteins and >70 RNAs. While we know that this machinery is absolutely essential for life, we have little understanding of the function of the individual players. To shed light on the function of these assembly factors, we use a combination of approaches – including biochemistry, mechanistic enzymology, yeast genetics, structural biology, and protein engineering. We have focused on assembly of the 40S subunit and have developed a recombinant system that recapitulates the final steps in assembly. This system now allows us to uncover new steps and dissect the role of individual proteins in these steps. Our ultimate goal is to understand the function of assembly factors, the order of events as well as the rationale for this order, aiming to delineate general principles important for the assembly of large RNA-protein complexes.
Diploma, Biochemistry, Witten/Herdecke University, 1998
Ph.D., Biochemistry, Stanford University, 2003
Diploma, Chemistry, Ruhr University Bochum, 1995
Ph.D., Stanford University, Daniel Herschlag
Postdoctoral work, UC Berkeley, Jennifer Doudna
University of Michigan, Department of Chemistry Seyhan Ege Professorship (2009) NSF CAREER Award (2009) University of Michigan, Biological Sciences Scholar Award (2006)
Young, C.L., Khoshnevis, S., and Karbstein, K. (2013). Co-factor dependent specificity of a DEAD-box protein. Proceedings of the National Academy of Sciences 110, E2668-2676.
Strunk, B.S., Novak, M.N., Young, C.L. and Karbstein, K. (2012). Joining of 60S subunits and a translation-like cycle in 40S ribosome maturation. Cell 150(1):111-21.
Strunk, B.S., Loucks, C.E., Su, M., Vashtish, H., Cheng, S., Schilling, J., Brooks, C.L. III Karbstein, K.# and Skiniotis, G.# (2011) Ribosome Assembly Factors Prevent Premature Translation Initiation by 40S Assembly Intermediates. Science 333(6048), 1449-53. # corresponding authors
Lamanna, A.C. and Karbstein, K.(2009). Nob1 uses its PIN domain to bind cleavage site D at the 3'-end of 18S rRNA. Proceedings of the National Academy of Sciences 106, 14259-14264.