Dr Monica Gerth

Research Fellow
  • Biochemistry Department
  • School of Biomedical Sciences
  • University of Otago
  • P.O. Box 56
  • 710 Cumberland St
  • Dunedin 9054 , New Zealand
  • Tel.: 64 3 479-7836
  • Fax: 64 3 479-7866
  • Email:monica.gerth@otago.ac.nz

Research Interests

  • Protein engineering and directed evolution.
    • Engineering biofilm-blocking enzymes.
  • Microbial chemotaxis.
    • Functional and structural diversity of bacterial chemoreceptors.
    • Phytophthora chemotaxis (e.g. Kauri dieback).

More information is available on our lab website.


B.Sc., The Evergreen State College, USA (2002). Ph.D., Emory University, USA (2007). FRST Postdoctoral Fellow, Massey University (2008-2012). 

Positions Available

Enquires about projects from prospective students are welcome and should be sent to monica.gerth@otago.ac.nz. Please include a CV and a decription of your research interests. Information on scholarships for postgraduate students can be found at the University of Otago's website at http://www.otago.ac.nz/study/scholarships/


Kopke, M., Patrick, W.M., Maddock, D.J. and Gerth, M.L. (2017) Enzyme-Altered Metabolite Activity. US patent No: US 9,550,979 B2. Granted 24 January, 2017. 


  • Danni Maddock
  • 2016, NZSBMB student poster competition, 1st place
  • Max Ehrhardt
  • 2016, NZSBMB student poster competition, 3rd place
  • Lottie Armstrong
  • 2016, NZMS student poster competition, 2nd place
  • Tom Wiggins
  • 2016, Maurice Wilkins Centre Early Career Symposium poster prize, 1st place
  • Dr Monica Gerth
  • 2014, Winner of the U. Otago Division of Health Sciences Translational Research Grant

Selected Publications

Carl H Mesarich, Jonathan Rees-George, Paul P Gardner, Fatemeh Ashari Ghomi, Monica L Gerth, Mark T Andersen, Erik H A Rikkerink, Peter C. Fineran, and Matthew D Templeton., Transposon insertion libraries for the characterization of mutants from the kiwifruit pathogen Pseudomonas syringae pv. actinidiae., PLoS ONE 2017 vol. 12 (3) p. e0172790., Link »

Brewster, J.L., McKellar, J.L.O., Finn, T.J., Newman, J., Peat, T.S. and Gerth, M.L. (2016) Structural basis for ligand recognition by a Cache chemosensory domain that mediates carboxylate sensing in Pseudomonas syringae. Scientific Reports, doi:10.1038/srep35198.

Maddock, D.J., Patrick, W.M. and Gerth, M.L. (2015) Substitutions at the cofactor binding sites of a clostridial alcohol dehydrogenase lead to unexpected changes in substrate specificity. Protein Engineering, Design, and Selection, 28: 251-258.

McKellar, J.L., Minnell, J.J. and Gerth, M.L. (2015) A high-throughput screen for ligand binding reveals the specificities of three amino acid chemoreceptors from Pseudomonas syringae pv. actinidiae. Molecular Microbiology, 96:694-707.

Kopke, M., Gerth, M.L., Maddock, D.J., Mueller, A.P., Liew, F.M., Simpson, S.D. and Patrick, W.M. (2014) Reconstruction of an acetogenic 2,3-butanediol pathway involving a novel NADPH-dependent primary-secondary alcohol dehydrogenase. Applied and Environmental Microbiology, 80: 3394-3403.

Patrick, W.M. and Gerth, M.L. (2014) ITCHY: Incremental Truncation for the Creation of Hybrid Enzymes. Methods in Molecular Biology, Directed Enzyme Evolution, 1179:225-244.

Wilson, R.H., Morton, S.K., Deiderick, H., Gerth, M.L., Paul, H.A., Gerber, I., Patel, A., Ellington, A.D., Hunicke-Smith, S.P. and Patrick, W.M. (2013). Engineered DNA ligases with improved activities in vitro. Protein Engineering, Design and Selection, 26, 471-478.

Gerth, M.L., Ferla, M.P. and Rainey, P.B. (2012) The origin and ecological significance of multiple branches for histidine utilization in Pseudomonas aeruginosa PAO1. Environmental Microbiology, 14: 1929-1940.

Gerth, M.L., Lutz, S. (2007) Non-homologous recombination of deoxyribonucleoside kinases from human and Drosophila melanogaster yields human-like enzymes with novel activities. Journal of Molecular Biology, 370: 742-751.

Gerth, M.L., Patrick, W.M., Lutz, S. (2004) A second-generation system for unbiased reading frame selection. Protein Engineering, Design and Selection, 17: 595-602.