Associate Professor Oliver Rackham

Laboratory Head, Synthetic Biology and Drug DiscoveryAssociate Professor Oliver Rackham
T:   +61 8 6151 0735

Associate Professor Rackham gained his Bachelor of Science and Doctorate in Biochemistry at the University of Otago, Dunedin, New Zealand. In 2003 Oliver relocated to the MRC Laboratory of Molecular Biology, UK, as an MRC Career Development Fellow, working with Professor Jason Chin on approaches to systematically re-engineer the genetic code.

Oliver established his own group at the Perkins (then WAIMR) in 2006 as an NHMRC Peter Doherty Fellow. Since then he has been awarded a Wenner-Gren Foundation Fellowship, an ARC Future Fellowship, the Marshall Medal, and was admitted to the European Inventor Hall of Fame. Oliver’s research is currently funded by grants from the ARC and NHMRC.

Research overview
Associate Professor Rackham‘s research falls into two areas of interest: engineering and understanding mammalian gene expression, and synthetic biology using microbial model organisms. His work focuses on developing new tools and therapeutics to target cancer, mitochondrial diseases and antibiotic-resistant bacteria.

Research projects

Synthetic Biology
One of the key aims of synthetic biology is to program cells with new functions. To achieve this aim it is necessary to create additional, new components that interact in a programmable manner, both with each other and with the existing cellular network. To engineer these components we have created a number of powerful new genetic selection approaches Synthetic-biologythat can be used to tailor the molecular specificities of genes, RNAs and proteins in bacteria and yeast. Current projects involve manipulating bacteria to efficiently express proteins containing selenium and engineering yeast to produce new antibiotics.

Mammalian Gene Expression
From synthesis to destruction, mRNAs are associated with an array of proteins. Proteins control the efficiency of transcription, processing, nuclear export, translation, localization and degradation of mRNA. The importance of regulation at the level of mRNA has become increasingly apparent with the discovery of disease causing defects in these processes. We are using synthetic biology and transcriptomic approaches to engineer and understand mammalian RNA-binding proteins for use as tools in biotechnology and as therapeutics for human diseases.

Selected publications

  1. Kuznetsova I, Siira SJ, Shearwood AJ, Ermer JA, Filipovska A, Rackham O. (2017) Simultaneous processing and degradation of mitochondrial RNAs revealed by circularized RNA sequencing. Nucleic Acids Research gkx104. doi: 10.1093/nar/gkx104  [NCBI PubMed Entry]
  2. Coquille S, Filipovska A, Chia T, Rajappa L, Lingford JP, Razif MF, Thore S, Rackham O. 2014. An artificial PPR scaffold for programmable RNA recognition. Nature Communications. 5:5729. [NCBI PubMed Entry]
  3. Thyer R, Filipovska A, Rackham O. 2013. Engineered rRNA enhances the efficiency of selenocysteine incorporation during translation. Journal of the American Chemical Society 135(1):2-5. [NCBI PubMed Entry]
  4. Filipovska A, Rackham O. 2012. Modular recognition of nucleic acids by PUF, TALE and PPR proteins. Molecular Biosystems 8(3):699-708. [NCBI PubMed Entry]
  5. Filipovska A, Razif MF, Nygård KK, Rackham O. 2011. A universal code for RNA recognition by PUF proteins. Nature Chemical Biology 7(7):425-7. [NCBI PubMed Entry]
  6. Filipovska A, Rackham O. 2011. Designer RNA-binding proteins: New tools for manipulating the transcriptome. RNA Biology 8(6):978–83. [NCBI PubMed Entry]
  7. Filipovska A, Rackham O. 2008. Building a parallel metabolism within the cell. ACS Chemical Biology 3(1):51-63. [NCBI PubMed Entry]
  8. Rackham O, Wang K, Chin JW. 2006. Functional epitopes at the ribosome subunit interface. Nature Chemical Biology 2(5):254-8. [NCBI PubMed Entry]
  9. Rackham O, Chin JW. 2005. Cellular logic with orthogonal ribosomes. Journal of the American Chemical Society 127(50):17584-5. [NCBI PubMed Entry]
  10. Rackham O, Chin JW. 2005. A network of orthogonal ribosome·mRNA pairs. Nature Chemical Biology 1(3):159-66. [NCBI PubMed Entry]
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