• PhD in Molecular Genetics (1999)
• BSc (Hons) 1995

Jo Morris qualified with a BSc (Hons) in Biology from the University of York in 1995. She went on to study for a PhD in cancer biology at the Imperial Cancer Research Fund in London. After post-doctoral research at King’s College London she was awarded a Fellowship by the Breast Cancer Campaign (also undertaken at King’s College London at Guy’s Hospital). In 2010 Jo joined the School of Cancer Sciences at the University of Birmingham, to help establish the Birmingham Centre for Genome Biology.

Her Laboratory focuses on cellular pathways associated with cancer development and predisposition, and their potential exploitation for treatment and diagnosis.

In 2009 Jo and her team were awarded ‘Research Team of the Year’ by the breast cancer research charity, Breast Cancer Campaign.

Jo won ’best invited speaker’ at the 2015 Breast Cancer Symposium.

Jo was promoted to Reader in 2013 and to Professor in 2016.

• Module Lead for Genomics on the Cancer Sciences MRes course
• BMedSci
• DNA damage pathways in human disease (UG)
• Advanced Molecular  Experimental Genetics
• Invasion and Metastasis Small group teaching (found Medical Pract Cancer)
• Introduction to Experimental Skills (UG)

Jo has current PhD students investigating:

• Targetting SUMO pathways for cancer treatment
• BRCA1 missense changes and the link to breast cancer.

Together with Rob Neely at the School of Chemistry she supervises a student investigating new ways of imaging DNA repair (funded by the EPSRC).

Potential self-funded PhD positions are open within the Morris Lab.

(Please see here for information of fees first http://www.birmingham.ac.uk/postgraduate/dr-fees/index.aspx then email Jo directly with your CV and research interest).

The work of the group has led to significant contributions identify roles for the small modifiers, ubiquitin and SUMO, in promoting DNA repair and in revealing their potential role in cancer predisposition. These small proteins can quickly change the way that proteins behave – and central requirement for a quick cellular response to damaged DNA, or a stalled replication fork.

We showed that ubiquitin conjugates are located to sites of double-stranded DNA breaks in mammalian cells and their dependency, in part, on the breast and ovarian cancer predisposition protein, BRCA1 (HMG 2004). Examination of the proteasomal deubiquitinating enzyme, POH1 showed it is a key regulator of ubiquitin at damaged chromatin, and controls the amplitude of the subsequent response and regulates a fast type of DNA repair, NHEJ (EMBO J 2012).

Recently the Morris group has shown, for the first time, how BRCA1 acts to oppose 53BP1 and promote homologous recombination, revealing that this ability requires BRCA1 to add ubiquitin to histones to activate the chromatin remodeller SMARCAD1 (NSMB, 2016, Nucleus 2016).

Our model of a disruptive, pleiotropic Brca1 variant (similar to a version found in breast cancer patients) combined with a model from collaborators at the NKI, was the first to recapitulate genetic events of familial breast cancer brought about BRCA1 N-terminal mutations (Cancer Cell 2011). The Brca1 N-terminus is required for genomic stability and tumour suppression but, unexpectedly, its tumours become resistant to agents targeting homologous recombination DNA repair.

In 2009 we were one of the first to report that SUMO regulates several aspects of the response to DNA damage (Nature 2009). SUMO-signalling, while still poorly understood, is now an accepted part of DNA damage signalling.  In 2013 we found that the SUMO protease SENP7 regulates chromatin state and permits DNA repair (EMBO R 2013).

Current and future work aims to establish how SUMO conjugation is activated in by DNA damage, and what SUMOylation does to the proteins it modifies. We aim to establish how BRCA1 protects cells from gene deletions and rearrangements in replication and how cells control the consequences of its E3 Ubiquitin ligase function.

Functions of BRCA1 and the implications for treatment -  Dr Morris speaks with ecancer at the 1^st Cancer Research @ Bath Symposium 

Jo is part of the Birmingham Centre for Genome Biology and also works with Colleges at the School of Chemistry.    

Jo also works with researchers at the NKI in the Netherlands: http://www.birmingham.ac.uk/research/activity/mds/centres/genome-biology/index.aspx            https://www.nki.nl/divisions/biochemistry/sixma-t-group/

and Colleges at the Sussex Genome Stability Centre.

Member of Breast Cancer Now Scientific Advisory Board (2015-2018)

Morris JR, Garvin AJ.  SUMO in the DNA Double-Stranded Break Response: Similarities, Differences and Co-operation with Ubiquitin.  J Mol Biol. 2017 May 17. pii: S0022-2836(17)30227-9. doi: 10.1016/j.jmb.2017.05.012. [Epub ahead of print].

Densham RM, Morris JR.  The BRCA1 Ubiquitin ligase function sets a new trend for remodelling in DNA repair.  Nucleus. 2016 Dec 29:1-10. doi: 10.1080/19491034.2016.1267092.

Densham RM, Garvin AJ, Stone HR, Strachan J, Baldock RA, Daza-Martin M, Fletcher A, Blair-Reid S, Beesley J, Johal B, Pearl LH, Neely R, Keep NH, Watts FZ, Morris JR.  Human BRCA1-BARD1 ubiquitin ligase activity counteracts chromatin barriers to DNA resection. Nat. Struct. Mol. Biol. 2016 Jul;23(7):647-55. doi: 10.1038/nsmb.3236.

Alexander J Garvin, Ruth M Densham, Sarah A Blair-Reid, Kenny M Pratt, Helen R Stone, Daniel Weekes, Kirsty J Lawrence and Joanna R Morris* The deSUMOylase SENP7 promotes chromatin relaxation for homologous recombination DNA repair.EMBO reports (2013), 14, - 975 - 983.

Butler LR, Densham RM, Jia J, Garvin AJ, Stone HR, Shah V, Weekes D, Festy F, Beesley J, Morris J.R.The proteasomal de-ubiquitinating enzyme POH1 promotes the double-strand DNA break response. EMBO J (Dec 2012) Oct 3;31(19):3918-34.

Drost, R., P. Bouwman, S. Rottenberg, U. Boon, E. Schut, S. Klarenbeek, C. Klijn, I. van der Heijden, H. van der Gulden, E. Wientjens, M. Pieterse, A. Catteau, P. Green, E. Solomon, J. R. Morris* and J. Jonkers*, BRCA1 RING Function Is Essential for Tumor Suppression but Dispensable for Therapy Resistance. Cancer Cell (Dec 2011) 20(6): 797-809.

Morris, J.R. More Modifiers Move on DNA Damage, Cancer Research (2010), 15;70(10):3861-3.

Morris, J.R.(2010) SUMO in the mammalian DNA damage response. Biochem Trans. ;38:92-7

Morris, J.R., Boutell, C., Keppler, K., Densham, R., Weekes, D., Alamshah, A., Butler, L., Galanty, Y., Pangon, L., Kiuchi, T., Ng, T. and Solomon, E. (2009) The SUMO modification pathway is involved in the BRCA1 response to genotoxic stress. Nature;462:886-90.

Solomon, E and Morris, J.R. (2009) Chapter 4. Recent advances in understanding the cellular functions of BRCA1. In Welcsh, P.L. (ed.), The Role of Genetics in Breast and Reproductive Cancers. New York, USA. Springer Science + Business Media and Humana Press

Alamshah, A., Springall, R., Gillett, C.E., Solomon, E. and Morris, J.R (2008) Use of a BRCA1 peptide validates MS110 as a BRCA1-specific antibody in immunohistochemistry. Histopathology, 53, 117-20.

Barwell, J., Pangon, L., Hodgson, S., Georgiou, A., Kesterton, I., Slade, T., Taylor, M., Payne, S.J., Brinkman, H., Smythe, J., Sebire, N.J., Solomon, E., Docherty, Z., Camplejohn, R., Homfray, T. and Morris, J.R. (2007) Biallelic mutation of MSH2 in primary human cells is associated with sensitivity to irradiation and altered RAD51 foci kinetics. J Med Genet, 44, 516-20.