Eckhard Jankowsky, Ph.D.

Assistant Professor

Department of Biochemistry

Curriculum Vitae

Research: Molecular Mechanism of RNA helicases

RNA helicases utilize ATP to remodel RNA and ribonucleoprotein complexes. RNA helicases are the largest group of enzymes in eukaryotic RNA metabolism and virtually all steps of cellular RNA processing involve members of this highly conserved protein family, which includes the DEAD, DEAH, and DExH (together DExH/D) subgroups. Despite their central biological roles, it is not well understood how RNA helicases function at the molecular level. Research in our laboratory seeks to illuminate molecular mechanism(s) and design principle(s) that enable these molecular motors to use one highly conserved core to carry out an astonishing multitude of biological functions. At this time, we focus our inquiry on two model enzymes: NPH-II from vaccinia virus and DED1 from Saccharomyces cerevisiae, and we utilize an interdisciplinary approach that includes molecular biology (yeast), biochemistry (gels), and single molecule fluorescence (lasers).

 

Selected Publications

Jankowsky E. (2005)
Helicase snaps back. (News and Views)
Nature 437:1245 (2005). /

Yang Q, Jankowsky E. (2005)
ATP- and ADP-dependent modulation of RNA unwinding and strand annealing activities by the DEAD-box protein DED1.
Biochemistry 44:13591-13601 (2005). /

Fairman ME, Maroney PA, Wang W, Bowers HA, Gollnick P, Nilsen TW, Jankowsky E. (2004)
Protein displacement by DExH/D “RNA helicases” without duplex unwinding.
Science 304:730-734 (2004). /

Jankowsky E, Gross C, Shuman S, Pyle AM.
Active disruption of an RNA-protein interaction by a DExH/D RNA helicase.
Science 291:121-125 (2001). /

Jankowsky E, Gross C, Shuman S, Pyle AM.
The DExH protein NPH-II is a processive and directional motor for unwinding RNA.
Nature 403: 447-451 (2000). /