Carnegie Mellon University

David Hackney

David Hackney

Professor of Biological Sciences

Research

The Hackney lab is concerned with the mechanisms, regulation and structure of enzymes, particularly how structure and mechanism are interrelated.  Emphasis is on how ATP hydrolysis is coupled energetically to processes such as motor proteins (kinesins) and nucleic acid helicases. We are currently studying (in collaboration with the De La Cruz lab at Yale) the mechanism of an RNA helicases and plan to extend this analysis to other RNA-dependent ATPases that are required for structural rearrangements of secondary and tertiary RNA structure.

Publications

Helicase papers:

Hackney, D.D. Oxygen Isotopic Exchange Probes of ATP Hydrolysis by RNA Helicases. In Eckhard Jankowsky, editor: Methods in Enzymology, Vol. 511, Burlington: Academic Press, 2012, pp. 65-74.

Cao, W.; Coman, M.M.; Ding, S.; Henn, A.; Middleton, E.R.; Bradley, M.J. Rhoades E; Hackney, DD; Pyle ,A.M.; De La Cruz, E.M. Mechanism of Mss116 ATPase Reveals Functional Diversity of DEAD-Box Proteins. J. Mol. Biol. 2011, 409, 399-414.

Henn, A.; Cao, W.; Licciardello, N.; Heitkamp, S. E.; Hackney, D. D.; De La Cruz, E. M. Pathway of ATP Utilization and Duplex RRNA Unwinding by the DEAD-Box Helicase, DbpA. Proc. Natl. Acad. Sci. U. S. A. 2010, 107, 4046-4050.

Henn, A.; Cao, W.; Hackney, D. D.; De La Cruz, E. M. The ATPase Cycle Mechanism of the DEAD-Box RRNA Helicase, DbpA. J. Mol. Biol. 2008, 377, 193-205.

Other areas:

Kaan, H.Y.; Hackney, D.D.; Kozielski, F. The Structure of the Kinesin-1 Motor-Tail Complex Reveals the Mechanism of Autoinhibition. Science 2011, 333, 883-885.

Hackney, D.D.; Baek, N.; Snyder, A.C. Half-site inhibition of dimeric kinesin head domains by monomeric tail domains. Biochemistry 2009, 48, 3448-3456.

Kaan, H.Y.; Ulaganathan, V.; Hackney, D.D.; Kozielski, F.; An Allosteric Transition Trapped in an Intermediate State of a New Kinesin-Inhibitor Complex. Biochem. J. 2009, 425, 55-60.

Hackney, D.D.; Stock, M.F. Kinesin tail domains and Mg2+ directly inhibit release of ADP from head domains in the absence of microtubules. Biochemistry 2008, 47, 7770-7778.

Hackney, D.D. Processive motor movement. Science 2007, 316, 58-59.

Olivares, A.O.; Chang, W.; Mooseker, M.S.; Hackney, D.D.; De La Cruz, E.M. The tail domain of myosin Va modulates actin binding to one head. J.Biol.Chem. 2006, 281, 31326-31336.