Dr Miriam Sharpe

Research Fellow
Miriam Sharpe3
  • Biochemistry Department
  • School of Biomedical Sciences
  • University of Otago
  • P.O. Box 56
  • 710 Cumberland St
  • Dunedin 9054 , New Zealand
  • Tel.: 64 3 479-5148
  • Fax: 64 3 479-7866
  • Email:miriam.sharpe@otago.ac.nz

Research:

Dr Sharpe studies the structure and function of proteins: revealing the structure of proteins in order to find out how they work, and to uncover more about their biology.

Current interests:

Bioluminescence

Proteins that catalyse the production of light, especially in the Japanese firefly squid (Watasenia scintillans), the New Zealand glowworm (Arachnocampa luminosa), and dinoflagellate marine plankton.

NZ glowworm

Firefly squid on the coastline bioluminescing blue

Firefly squid, Toyama Bay, Japan

Drug Targets

Elucidating the structures of proteins that are potential drug targets for future structure-based drug design efforts. For example:

  • Proteins that are implicated in cancer and are important in epigenetics and chromatin remodelling, such as the histone-modifying Polycomb group complex PRC2.
  • Proteins from microbial pathogens, such as Mycobacterium tuberculosis, Streptococcus pneumoniae and Candida albicans.

Research opportunities

Expressions of interest are welcome for postgraduate research projects, and should be sent to Dr Miriam Sharpe.

Information about postgraduate study at the University of Otago and scholarships available can be found at the University of Otago's postgraduate and scholarship pages.

University of Otago postgraduate page

University of Otago scholarships page

Selected Publications

Gimenez G, Metcalf P, Paterson NG & Sharpe ML, Mass spectrometry analysis and transcriptome sequencing reveal glowing squid crystal proteins are in the same superfamily as firefly luciferase, Scientific Reports 6: 27638,

Miriam L Sharpe, Peter K Dearden, Gregory Gimenez, and Kurt L Krause., Comparative RNA seq analysis of the New Zealand glowworm Arachnocampa luminous reveals bioluminescence-related genes., BMC Genomics 2015 vol. 16 (1) p. 825, Link »

Sharpe ML, Hastings JW, Krause KL, Luciferases and light-emitting accessory proteins: structural biology, eLS John Wiley & Sons, Ltd. (2014), Link »

Im H, Sharpe ML, Strych U, Davlieva M, Krause KL, The crystal structure of alanine racemase from Streptococcus pneumoniae, a target for structure-based drug design, BMC Microbiology (2011) 11:116, Link »

Patrick WM, Nakatani Y, Cutfield SM, Sharpe ML, Ramsay RJ, Cutfield JF, Carbohydrate binding sites in Candida albicans exo-?-1,3-glucanase and the role of the Phe-Phe ‘clamp’ at the active site entrance, FEBS Journal (2010) 277(21): 4549-4561, Link »

Margueron R, Justin N, Ohno K, Sharpe ML, Son J, Drury WJ, Voigt P, Martin S,
Taylor WR, De Marco V, Pirrotta V, Reinberg D, Gamblin SJ, Role of the polycomb protein EED in the propagation of repressive histone marks, Nature (2009) 461: 762-767, Link

Sharpe ML, Gao C, Kendall SL, Baker EN, Lott JS, The structure and unusual protein chemistry of Hypoxic Response Protein 1, a latency antigen and highly expressed member of the DosR regulon in Mycobacterium tuberculosis, Journal of Molecular Biology (2008) 383 (4): 822-836, Link

Sharpe ML, Baker EN, Lott JS, Crystallization of a protein using dehydration without a precipitant, Acta Crystallographica Section F (2005) F61: 565-568, Link

Sharpe M, Love C, Marshall C, Lactate dehydrogenase from the Antarctic eelpout, Lycodichthys dearborni, Polar Biology (2001) 24 (4): 258-269, Link