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  • 16/05/2016
    Mnika Allison Danni
    Three of the four travel grants recently awarded by the New Zealand Society for Biochemistry and Molecular Biology went to Otago Biochemistry students.
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  • 13/05/2016
    Four projects in the Department of Biochemistry were successful in the latest round of Lotteries Health funding, and Professor Peter Dearden won $137,821 in the Unlocking Curious Minds Contestable Fund.
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  • 29/04/2016
    SinothaiBiochemJ cover
    The work Sinothai Poen published as part of his recent PhD has been chosen as the cover of the journal Biochemical Journal this month. Sinothai did his PhD with Professor Kurt Krause, and has since returned to Thailand to take up a lecturing position.
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  • Featured publication

    James M Murphy, Yoshio Nakatani, Sam A Jamieson, Weiwen Dai, Isabelle S Lucet, and Peter D Mace., Structure, 2015 vol. 23 (11) pp. 2111-2121

    TRIB1 is part of the protein family Tribbles, which play diverse roles in cell signalling and development. Tribbles are named after the small, furry creatures from Star Trek that reproduce uncontrollably. Tribbles are unusual types of proteins called pseudokinases, which have been described as ‘dead’ enzymes because their structures evolved to leave them incapable of catalysing chemical reactions. The researchers used powerful X-ray beams at the Australian Synchrotron to obtain the three-dimensional structure of Trib1, revealing that it is hugely contorted compared to related proteins that do function as catalysts. Instead of driving chemical reactions Trib1 acts as a scaffold to bring many proteins together, and the team discovered how Trib1 recruits specific proteins to be degraded. In the future it is hoped that the structure of Trib1 could help in developing new drugs to treat cancers such as acute myeloid leukaemia (AML), which can be caused by excess Trib1 protein driving abnormal production of white blood cells.

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