Dr Esther Bulloch

2005 Ph.D. in Biological Chemistry, University of Cambridge, United Kingdom, Supervisor: Prof Chris Abell. 2000 B.Sc. (1st class Hons.) in Chemistry and Biochemistry, Massey University, NZ. Supervisor: Dr Emily Parker.

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Research Fellow

Biography

Esther completed her PhD in Biological Chemistry at the University of Cambridge in 2005 with Dr Chris Abell and then spent one year as a postdoctoral researcher at Ohio State University.  In 2006 she returned to New Zealand to join the Structural Biology Group at the University of Auckland, initially working with Prof. Ted Baker and Dr Shaun Lott.  In 2010 she joined the lab of Dr Richard Kingston as a Minstry of Science postdoctoral fellow to study protein folding and structural domains.  Since 2017 she has been an associate investigator on a Marsden-funded project studying communication networks in enzymes in collaboration with Dr Jodie Johnston (University of Canterbury) and Dr Ghader Bashiri (University of Auckland).

Research | Current

Protein folding
In collaboration with Dr Richard Kingston I am studying how a small protein domain transitions from a molten globule to a fully folded state.  We are studying the "foot" domain of the RNA-dependent RNA polymerase of mumps virus which is thought to assist the polymerase in "walking" along the viral genome during replication.  In solution this protein domain exists in a disordered molten globule state but as part of its function it is able to attain a three-helix bundle structure.  By adding in chemical stabilisers we are also able to make this protein domain transition from a molten globule to a fully folded state and examine the intermediate steps.  Using NMR spectroscopy, combined with other biophysical techniques, we are able to obtain atom specific details on this folding pathway. 

Characterising a new biochemical pathway from the kiwifruit pathogen Psa

Pseudomonas syringae pv. actinidiae (Psa) has had a major effect of kiwifruit crops in New Zealand in recent years.  In collaboration with Assoc. Prof. Matt Templeton (Plant and Food Research, and University of Auckland) we are studying a new biochemical pathway from Psa that appears to be associated with particularly devastating variants of this pathogen.  This pathway is derived from chorismate and our hypothesis is that it produces a secondary metabolite involved in plant-pathogen interactions.  Since the product can not be predicted based on bioinformatics, we are currently stepping through each enzyme in the pathway to determine its function and ultimately identify the final product. 

Communication networks in enzymes

With Dr Jodie Johnston (University of Cantebury) and Dr Ghader Bashiri (University of Auckland) I am studying how information is communicated within an enzyme complex.  We are using an enzyme from the menaquinone biosynthesis pathway in Mycobacterium tuberculosis as a model system.  MenD is reponsible for the second committed step of the menanquinone biosynthesis pathway and exists as tetramer in solution.  We observe communication between the four active sites of this complex, and between the active sites and inhibitor binding sites.  Currently we are attempting to unpick the communicate networks that faciltate this cooperative behaviour using structural studies, site-directed mutagenesis, activity assays and molecular modelling.  

 

Postgraduate supervision

Former students

PhD students

Joint supervisor of PhD candidate Nicole Herr (completed 2019)

 

Masters students

Claudia Hadfield (completed 2017)

 

BSc(Hons) students

Lucy Mitsugi-McHattie (2019)

Claudia Hadfield (2015)

Sungmin Chi (2010)

Selected publications and creative works (Research Outputs)

  • Jirgis, E. N. M., Bashiri, G., Bulloch, E. M. M., Johnston, J. M., & Baker, E. N. (2016). Structural views along the Mycobacterium tuberculosis MenD reaction pathway illuminate key aspects of thiamin diphosphate-dependent enzyme mechanisms. Structure, 24 (7), 1167-1177. 10.1016/j.str.2016.04.018
    Other University of Auckland co-authors: Jodie Johnston, Ghader Bashiri
  • Bashiri, G., Johnston, J. M., Evans, G. L., Bulloch, E. M. M., Goldstone, D. C., Jirgis, E. N. M., ... Manos-Turvey, A. (2015). Structure and inhibition of subunit I of the anthranilate synthase complex of Mycobacterium tuberculosis and expression of the active complex. Acta Crystallographica Section D: Biological Crystallography, 71, 2297-2308. 10.1107/S1399004715017216
    Other University of Auckland co-authors: Ghader Bashiri, Jodie Johnston, David Goldstone, Rochelle Ramsay, Shaun Lott
  • Chai, A.-F., Bulloch, E. M., Evans, G. L., Lott, J. S., Baker, E. N., & Johnston, J. M. (2015). A covalent adduct of MbtN, an acyl-ACP dehydrogenase from Mycobacterium tuberculosis, reveals an unusual acyl-binding pocket. Acta Crystallographica Section D: Biological Crystallography, 71 (Pt 4), 862-872. 10.1107/S1399004715001650
    Other University of Auckland co-authors: Jodie Johnston, Shaun Lott
  • Evans, G. L., Gamage, S. A., Bulloch, E. M. M., Baker, E. N., Denny, W. A., & Lott, J. S. (2015). Corrigendum: Repurposing the Chemical Scaffold of the Anti-Arthritic Drug Lobenzarit to Target Tryptophan Biosynthesis in Mycobacterium tuberculosis. Chembiochem : a European journal of chemical biology, 16 (5)10.1002/cbic.201500098
    Other University of Auckland co-authors: Swarna Gamage, Bill Denny, Shaun Lott
  • Bulloch, E. M. M., & Kingston, R. L. (2014). Identifying protein domains by global analysis of soluble fragment data. Analytical Biochemistry, 465, 53-62. 10.1016/j.ab.2014.06.021
    Other University of Auckland co-authors: Richard Kingston
  • Rennie, M. L., McKelvie, S. A., Bulloch, E. M. M., & Kingston, R. L. (2014). Transient dimerization of Human MxA promotes GTP hydrolysis, resulting in a mechanical power stroke. Structure, 22 (10), 1433-1445. 10.1016/j.str.2014.08.015
    Other University of Auckland co-authors: Richard Kingston
  • Cookson, T. V. M., Castell, A., Bulloch, E. M. M., Evans, G. L., Short, F. L., Baker, E. N., ... Parker, E. J. (2014). Alternative substrates reveal catalytic cycle and key binding events in the reaction catalysed by anthranilate phosphoribosyltransferase from Mycobacterium tuberculosis. Biochem J, 461 (1), 87-98. 10.1042/BJ20140209
    Other University of Auckland co-authors: Shaun Lott
  • Evans, G. L., Gamage, S. A., Bulloch, E. M. M., Baker, E. N., Denny, W. A., & Lott, J. S. (2014). Repurposing the chemical scaffold of the anti-arthritic drug Lobenzarit to target tryptophan biosynthesis in Mycobacterium tuberculosis. Chembiochem, 15 (6), 852-864. 10.1002/cbic.201300628
    Other University of Auckland co-authors: Shaun Lott, Bill Denny, Swarna Gamage

Contact details

Primary office location

THOMAS BUILDING - Bldg 110
Level 3, Room 338
3 SYMONDS ST
AUCKLAND CENTRAL
AUCKLAND 1010
New Zealand