Professor Vic Arcus
Professor (Biological Sciences)
Qualifications: BSc, MSc Waikato, PhD Cambridge
Research and postgraduate study are encouraged in the Department of Biological Sciences. All research students acquire basic research skills and a knowledge of techniques, as well as training in specialist disciplines.
Our research focuses on molecular biology, structural biology and protein engineering. We are interested in the three-dimensional structures of several protein families and we use this information to study their biochemical functions. We use X-ray crystallography, protein NMR and other biophysical techniques. We are also interested in protein engineering to manipulate the structure and function of proteins. Here, we use site-directed mutagenesis and combinatorial mutagenesis in combination with structure determination to engineer new proteins.
Structural and Functional Biology of Microbial Toxin-Antitoxin Networks
Toxin-antitoxin pairs in bacteria act in concert to maintain low-copy number plasmids in daughter cells. It is also thought that these protein pairs are involved in microbial growth arrest under conditions of nutrient starvation and stress. We are pursuing the structures of a number of toxin-antitoxin complexes in an effort to find out more about the mechanism of cell-cycle arrest in Mycobacterium tuberculosis and M. bovis.
Protein Engineering to Produce Artificial Antibodies
We use a common protein scaffold to engineer a library of variants by randomizing up to seventeen amino acid positions on one face of the protein. We can then pick variants with desirable traits out of this library using phage display. This process is analogous to the selection of recombinant antibodies with the advantage that our scaffold is small and thermostable. Potential biotechnology applications are the current focus of our efforts.
Structural Biology of Proteins Involved in Plant Flowering
We are interested in several proteins which serve as checkpoints in triggering photoperiodic flowering in plants and their relationship with circadian controlled processes. We are using a range of biophysical techniques including X-ray crystallography, NMR, circular dichroism and electron microscopy to look at the structure and function of these proteins. Currently we are focusing on the proteins GI, FT and CO.
Endophyte Non-Ribosomal Peptide Sythetases
Very recently, our collaborators at AgResearch and Massey University have identified large operons in the symbiotic fungus Neotyphodium lollii, which code for non-ribosomal peptide sythetases. These genes code for proteins which are responsible for the biosynthesis of the important secondary metabolites. We are determining the structures of a number of domains from these operons to look at the molecular details of the biosynthesis of peramine.
- Chonira, Vikas (in progress). Engineering of an OB-fold protein scaffold for molecular recognition of cancer-specific intracellular kinases.
- Vickers, Chelsea (in progress). Determining the function and regulation of the prokaryotic VapBC toxin-antitoxin protein complexes.
- Cumming, Mathew (2012). Structure and Function of bacterially expressed soluble human ecto-nucleoside triphosphate diphosphohydrolase 1 (s-NTPDase1/s-CD39)
- Hennebry, Alexander (in progress). Identifying the signalling pathway of a novel splice-variant of myostatin
- Andrews (nee Littlejohn), Emma (2013). Biochemistry and biology of Pin domain proteins in TB
- Oulavallickal, Tifany (in progress). Reconstruction of aroa/mura ancestral enzymes and screening of potential inhibitors.
- Summers, Emma (2013). The biochemistry and structural biology of Lsr2 from Mycobacterium tuberculosis
- McKenzie, Joanna (2011). Structure & Function of PIN-Domain Toxin-Antitoxin Protein Arrays
- Ruthe, Alaine (in progress). The role of the toxin-antitoxin repertiore in pathogen survival and persistence
- Steemson, John (2011). Directed Evolution of a Protein Domain using Protein Engineering
- Till, Marisa (2011). Structural and Functional Investigation of Cellulase Enzymes from the Ruminant Bacterium Clostridium proteoclasticum
- Prentice, Erica (in progress). Ancestral enzyme reconstruction of LeuB
- Duyestyn, Jo (2012) The Function of VapC: Determining the mechanism and specificity of an RNase
- McMillan, Joel (2013) Biochemical characterisation of reconstructed ancestral CM-DAH7PS enzymes
- Sharrock, Abigail (2013) Characterisation of VapBC toxin-antitoxins from Mycobacterium tuberculosis
- Easter, Ashley (2010). Decoupling enzyme catalysis from thermal denaturation
Molecular biology; structural biology; protein engineering.
- Groussin, M., Hobbs, J., Szoellosi, G., Gribaldo, S., Arcus, V., Gouy, M. (2015) Toward more accurate ancestral protein genotype-phenotype reconstructions with the use of species tree-aware gene trees
Refereed journal article - Molecular Biology and Evolution
- Andrews, E., Arcus, V. (2015) The mycobacterial PhoH2 proteins are type II toxin antitoxins coupled to RNA helicase domains
Refereed journal article - Tuberculosis
- Arcus, V., Pudney, C. (2015) Change in heat capacity accurately predicts vibrational coupling in enzyme catalyzed reactions
Refereed journal article - FEBS Letters
- Newton, M., Arcus, V., Patrick, W. (2015) Rapid bursts and slow declines: on the possible evolutionary trajectories of enzymes
Refereed journal article - Journal of the Royal Society Interface
View All research publications by Vic Arcus
Contact DetailsEmail: firstname.lastname@example.org
Phone: +64 7 838 4679