Our JCB paper on prion-like domains is out …

Congratulations to Sven and Geraldine, and all the other authors … Hennig et al (2015) “Prion-like domains in RNA binding proteins are essential for building subnuclear paraspeckles” http://jcb.rupress.org/content/210/4/529.short with a very interesting commentary from Karla Neugebauer here: http://jcb.rupress.org/content/210/4/527.full

Posted on August 24th, 2015

Calling potential summer, honours and graduate students

Now’s the time to be thinking about your research future, ready for 2016. Have a look here: http://bondxray.org/opportunities.html.
UWA Biochem undergrads should look at the “Ivan T Oliver” scholarships for summer vacations.

Posted on August 12th, 2015

Our paper came out in Science!

Our paper on KAI2 proteins from parasitic weeds that detect strigolactone molecules secreted by nearby juicy crop plants was published in Science. Congratulations to Rohan – possibly the best outcome of a PhD side-project ever. Thanks to Dave Nelson and Caitlin Conn at Univ Georgia Athens for leading the project!


Posted on August 12th, 2015

The cytidine deaminase signature HxE (x) nCxxC of DYW1 binds zinc and is necessary for RNA editing of ndhD-1

Clement Boussardon, Alexandra Avon, Peter Kindgren, Charles S Bond, Michael Challenor, Claire Lurin, Ian Small. New Phytologist 203 (4), 1090-1095

In flowering plants, RNA editing involves deamination of specific cytidines to uridines in both mitochondrial and chloroplast transcripts. Pentatricopeptide repeat (PPR) proteins and multiple organellar RNA editing factor (MORF) proteins have been shown to be involved in RNA editing but none have been shown to possess cytidine deaminase activity. The DYW domain of some PPR proteins contains a highly conserved signature resembling the zinc-binding active site motif of known nucleotide deaminases. We modified these highly conserved amino acids in the DYW motif of DYW1, an editing factor required for editing of the ndhD-1 site in Arabidopsis chloroplasts. We demonstrate that several amino acids of this signature motif are required for RNA editing in vivo and for zinc binding in vitro. We conclude that the DYW domain of DYW1 has features in common with cytidine deaminases, reinforcing the hypothesis that this domain forms part of the active enzyme that carries out RNA editing in plants.

Posted on August 12th, 2015

Crystal ‘Unengineering': Reducing the Crystallisability of Sulfolobus solfataricus Hjc

CL Middleton, JL Parker, GJ Knott, MF White, CS Bond Australian Journal of Chemistry. http://dx.doi.org/10.1071/CH14342
The protein Hjc from the thermophilic archaeon Sulfolobus solfataricus (Ss) presented many challenges to both structure solution and formation of stable complexes with its substrate, the DNA four-way or Holliday junction. As the challenges were caused by an uncharacteristically high propensity for rapid and promiscuous crystallisation, we investigated the molecular cause of this behaviour, corrected it by mutagenesis, and solved the X-ray crystal structures of the two mutants. Characterisation and comparative analysis of the structures are presented along with discussion of the pitfalls of the use of protein engineering to alter crystallisability while maintaining biological function.

Posted on August 12th, 2015