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Murray Edwards College
University of Cambridge
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    Dr Aleksandra A Watson

    Murray Edwards College
    New Hall
    University of Cambridge
    Cambridge
    CB3 0DF

    Maplethorpe Fellow in Biochemistry; Director of Studies; Tutor

    Biochemistry

    Fellow

    Degrees and honours

    • PhD (by Incorporation) Cantab
    • DPhil Oxon
    • MBiochem Oxon (Hons)

    Research interests

    Aleksandra received a Sir Henry Wellcome Postdoctoral Fellowship based at the Biochemistry Department to study the regulation of DNA packaging into a compartment 40,000 times smaller. This packaging renders DNA inaccessible to essential processes involved in cell development and cancer progression, and must be tightly controlled.

    Biography

    Aleksandra received an MBiochem in Molecular and Cellular Biochemistry from Oxford University and completed her DPhil in the Department of Clinical Medicine at the same institution. Here, Aleksandra investigated the structural nature of protein-protein interactions in immune surveillance.

    Aleksandra teaches Part IA Natural Sciences, Medicine and Veterinary Medicine undergraduates, and is the Maplethorpe Fellow in Biological Sciences. Aleksandra is also the Director of Studies for Part IA and IB Biological Natural Sciences and Part II-III Biochemistry.

    Publications

    1. MICA Expression Is Regulated by Cell Adhesion and Contact in a FAK/Src-Dependent Manner. Moncayo G, Lin D., McCarthy M.T., Watson A.A., O'Callaghan C.A.

    Front Immunol. 2017 Jan 19;7:687. doi: 10.3389/fimmu.2016.00687. eCollection 2016. Included in the e-book NK Cells in Human Diseases: https://www.frontiersin.org/research-topics/4823/nk-cells-in-human-diseases-friends-or-foes.

    2. Architecture of TAF11/TAF13/TBP complex suggests novel regulation properties of general transcription factor TFIID. Gupta K., Watson A.A., Baptista T., Scheer E., Chambers A.L., Koehler C., Zou J., Obong-Ebong I., Kandiah E., Temblador A., Round A., Forest E., Man P., Bieniossek C., Laue E.D., Lemke E.A., Rappsilber J., Robinson C.V., Devys D., Tora L., Berger I. Elife. 2017 Nov 7;6. pii: e30395. doi: 10.7554/eLife.30395.

    3. Edlich-Muth C., Artero J.B., Callow P., Przewloka M.R., Watson A.A., Zhang W., Glover D.M., Debski J., Dadlez M., Round A.R., Forsyth V.T., Laue E.D. The Pentameric Nucleoplasmin Fold Is Present in Drosophila FKBP39 and a Large Number of Chromatin-Related Proteins. J Mol Biol. 2015 May 22;427(10):1949-63. doi: 10.1016/j.jmb.2015.03.010. Epub 2015 Mar 24.

    4. Alqarni S.S.M., Murthy A., Zhang W., Przewloka M.R., Silva A.P.G., Watson A.A., Lejon S., Pei X.Y., Smits A.H., Kloet S.L., Wang H., N.E., Stokes P.H., Blobel G.A., Vermeulen M., Glover D.M., Mackay J.P., Laue E.D. (2014). Insight into the architecture of the NuRD complex: Structure of the RbAp48-MTA1 sub-complex. J Biol Chem. Aug 29; 289 (35).

    5. Zhang W., Tyl M., Ward R., Sobott F., Maman J., Murthy A.S., Watson A.A., Fedorov O., Bowman A., Owen-Hughes T., El Mkami H., Murzina N.V., Norman D.G., Laue E.D. (2013). Structural plasticity of histones H3-H4 facilitates their allosteric exchange between RbAp48 and ASF1. Nat Struct Mol Biol. 2013 Jan;20(1):29-35.

    6. Watson A.A., Mahajan P, Mertens H.D., Deery M.J., Zhang W, Pham P, Du X, Bartke T, Zhang W, Edlich C, Berridge G, Chen Y, Burgess-Brown N.A., Kouzarides T, Wiechens N, Owen-Hughes T, Svergun D.I, Gileadi O, Laue ED. (2012). The PHD and Chromo Domains Regulate the ATPase Activity of the Human Chromatin Remodeler CHD4. J Mol Biol. Sep 7;422(1):3-17.

    7. Watson A.A., O'Callaghan C.A. (2011). Molecular Analysis of the Interaction of the Snake Venom Rhodocytin with the Platelet Receptor CLEC-2. Toxins. Aug;3(8):991-1003.

    8. Watson, A.A., Christou, C.M., O’Callaghan, C.A. (2011). Expression, purification and crystallization of the human UL16-binding protein ULBP1. Protein Expr Purif. Sep;79(1):44-8.

    9. Watson, A.A., Lebedev, A.A., Hall, B.A., Fenton-May, A.E., Vagin, A.A., Dejnirattisai, W., Mongkolsapaya, J., Felce, J., Screaton, G.R., Murshudov, G.N, O’Callaghan, C.A. (2011). Structural flexibility of the macrophage Dengue virus receptor CLEC5A: implications for ligand binding and signaling. J Biol Chem. Jul 8;286(27):24208-18. F1000 recommended.

    10. Watson, A.A., and O'Callaghan, C.A. (2009). Crystallization and X-ray diffraction analysis of human CLEC5A (MDL-1) - a Dengue virus receptor. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Jan 1;66(Pt 1):29-31.

    11. Watson, A.A., Christou, C.M., James, J.R., Fenton-May, A.E., Moncayo, G.E., Mistry, A.R., Davis, S.J., Gilbert, R.J., Chakera, A., O’Callaghan, C.A. (2009).The Platelet Receptor CLEC-2 is Active as a Dimer. Biochemistry. Nov 24;48(46):10988-96.

    12. Watson, A.A., and O'Callaghan, C.A. (2009). CLEC5. UCSD-Nature Molecule Pages. doi:10.1038/mp.a004147.01.

    13. O'Callaghan, C.A., Watson, A.A., Fenton-May, A.E., Christou, C.M. (2009). Structure and function of the activating receptor CLEC-2. Journal of Immunology. 182, 134.10.

    14. Watson, A.A., Fenton-May, A.E., Christou, C.M., and O'Callaghan, C.A. (2008). Structure and function of the CLEC-2 receptor and its ligands: 2.4. Immunology. 125 Supplement 1:13.

    15. Watson, A.A., Eble, J.A., and O'Callaghan, C.A. (2008). Crystal structure of rhodocytin, a ligand for the platelet-activating receptor CLEC-2. Protein Sci. 17, 1611-1616.

    16. Christou, C.M., Pearce, A.C., Watson, A.A., Mistry, A.R., Pollitt, A.Y., Fenton-May, A.E., Johnson, L.A., Jackson, D.G., Watson, S.P., and O'Callaghan, C.A. (2008). Renal cells activate the platelet receptor CLEC-2 through podoplanin. Biochem J. 411, 133-140.

    17. Watson, A.A., Brown, J., Harlos, K., Eble, J.A., Walter, T.S., and O'Callaghan, C.A. (2007). The crystal structure and mutational binding analysis of the extracellular domain of the platelet-activating receptor CLEC-2. J Biol Chem. 282, 3165-3172.

    18. Watson, A.A., and O'Callaghan, C.A. (2005). Crystallization and X-ray diffraction analysis of human CLEC-2.Acta Crystallograph Sect F Struct Biol Cryst Commun. 61(Pt 12), 1094-1096.