Nuclear Magnetic Resonance Dr Max Keniry

We apply the powerful technique of nuclear magnetic resonance (NMR) spectroscopy to highly complex problems in biology. Our main aim is to deduce the function of biological molecules and complexes from knowledge of their structure and dynamics at the atomic level.

We are primarily interested in proteins and nucleic acids and how they interact with one another. Understanding the mechanism of control of DNA replication and regulation of gene expression are important for studying the chemistry and biology of cancer and developing new anticancer drugs.

NMR spectroscopy is a rapidly developing technology and we frequently have to adapt and develop this technology in order to solve the complex structural problems presented by biological macromolecules. We also contribute to the development of NMR technology by devising and testing more efficient radiofrequency pulses and pulse shapes.

Current research activities

DNA quadruplexes

Normally DNA occurs in the well-known double helix structure. Recently it has been discovered that DNA also forms unusual structures such as quadruplexes. DNA quadruplexes appear to play a role in capping and protecting the ends of chromosomes as well as regulating the expression of genes, including some that are over-expressed in cancer cells. We are studying the structure of DNA quadruplexes and the mechanisms by which they fold and unfold. This information may lead to the development of anticancer drugs.

ESX - a protein implicated in breast cancer

ESX is a protein that belongs to the Ets family of transcription factors. The ESX transcription factor may have a role in the activation of the HER2/neu oncogene which is over-expressed in over 40% of breast tumours. We are studying the structure of ESX using NMR and X-ray crystallography.

DNA binding proteins

We are investigating the structure and function of proteins that interact with DNA, in particular the bacterial enzyme DNA polymerase III. The catalytic core of DNA polymerase III contains three tightly associated subunits (α , ε and θ). The θ subunit is the smallest, but the least understood of the three. Our group recently determined the structure of this subunit and we are now investigating its interaction with the other subunits to further understand how the enzyme functions.

Annual Research Report   (PDF format)

Group members

Academic Staff:
Dr Max Keniry (Leader)   |   Pavel Prosselkov

Technical and General Staff:
Elisabeth Owen

Key publications

1. Keniry, M. A., Strahan, G., Owen, E. A. and Shafer, R. H., The solution structure of the Na⁺ form of the dimeric G-quadruplex, [d(G₃T₄G₃)]₂ , Eur. J. Biochem., 233, 631-643 (1995).
2. Keniry, M. A., Owen, E. A. and Shafer, R. H., The three dimensional structure of the 4:1 Mithramycin:d(ACCCGGGT)₂ complex: Evidence for an interaction between the E Saccharides, Biopolymers, 54, 104-114 (2000).
3. Laajoki, L. G., Francis, G. L., Wallace, J. C., Carver, J. A. and Keniry, M. A., The solution structure and backbone dynamics of Long-[Arg3] Insulin-Like Growth Factor-I, J. Biol Chem., 275, 10009-10015 (2000).
4. Keniry, M. A., Berthon, H. A., Yang, J., Miles, C. S., and Dixon , N. E., The NMR solution structure of the θ subunit of DNA polymerase III from Escherichia coli, Protein Science, 9, 721-733 (2000).
5. Keniry, M. A., Quadruplex structures in nucleic acids, Biopolymers, 56, 123-146 (2001).

>>more publications

Max Keniry came to the ANU from the University of California, San Francisco, where he held a non-tenured Faculty position. He has been the Facility Coordinator of the University NMR Centre at the ANU and is now a Fellow at RSC and Head of the University NMR Centre.

Dr M A Keniry Research School of Chemistry, Building 35 Australian National University Canberra ACT 0200 AUSTRALIA Ph: +61 2 6125 2863 Fx: +61 2 6125 0750 E-mail: mkeniry@rsc.anu.edu.au