
Dr Felicity Watts
| Post: | Reader in Biochemistry (Genome Damage and Stability) |
| Location: | Genome Centre G4.12 |
| Email: | F.Z.Watts@sussex.ac.uk |
Telephone numbers | |
| Internal: | 8257 or 7512 |
| UK: | (01273) 678257 or (01273) 877512 |
| International: | +44 1273 678257 or +44 1273 877512 |
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Biography
1997-present Reader in Biochemistry (Sussex), 1995-1997 Senior Lecturer (Sussex), 1986-1995 Lecturer (Sussex), 1984-1986 Research Assistant Dept Genetics University of Leicester, 1981-1983 Research Assistant with Jean Beggs CRC Imperial College London, 1977-1980 PhD Biochemistry with Irving Johnston University College London, 1974-1977 BSc (Hons) Biochemistry University College London
Key responsibilities:
Course Organiser - Molecular Genetics
Member Biochemistry Exam Board
For Further details see:
http://www.sussex.ac.uk/lifesci/wattslab/index
For Publications see
Introduction
Failure to maintain genetic integrity can result in the inheritance of mutations, genetic disorders, cancer or cell death. To ensure genome stability, cells have evolved a number of different ways to deal with DNA damage. These include several DNA repair pathways capable of recognising and repairing different types of damage, and checkpoint mechanisms that arrest the cell cycle to prevent cells from entering the next phase of the cycle with DNA damage or unreplicated chromosomes.
Dissecting the role of the DNA integrity checkpoint protein Crb2
Crb2 is a key player in the DNA integrity checkpoint process in S. pombe (Willson et al., 1997) . It has two BRCT domains. It is related to the mammalian proteins BRCA1 (mutations in which result in a high proportion of breast and ovarian cancers) and 53BP1 (a protein that binds the tumour suppressor protein p53) both of which also contain two BRCT domains. While it is known that these proteins have important cellular roles, the nature of the contribution of the BRCT domains to their function remains largely unknown. We have recently elucidated the structure of the BRCT domains in Crb2 (Kilkenney et al., 2008). Using information gained form this structure we are currently analysing the role of the BRCT domains and proteins with which they interact.
Role of SUMO in maintenance of genetic integrity
SUMO is a small ubiquitin-like protein that is covalently attached to target proteins. Sumoylation can affect protein localisation, enzymatic activity, protein-protein and protein-DNA interactions. It can also target proteins for ubiquitination and subsequent degradation for the proteasome. Through the analysis of mutants defective in sumoylation we have demonstrated that SUMO is likely to have multiple roles in maintaining genetic integrity. For example, we have shown that several DNA replication, recombination and checkpoint proteins are SUMO modified (e.g. Rad22 (Ho et al, 2001) and Smc5-6 (Andrews et al, 2005), Rqh1, Mre11 (Watts 2008)). We have also identified two S. pombe SUMO ligases, Nse2 and Pli1 (Andrews et al, 2005). Nse2 is a component of the Smc5/6 complex and is essential for viability. Pli1 is not essential for viability despite having dramatically reduced levels of sumoylation. We are currently analysing the different roles of Nse2 and Pli1 in maintaining genetic integrity.
Dr Felicity Watts' GDSC Staff Profile www.sussex.ac.uk/gdsc/1-4-13.html
Molecular Genetics - lectures (Final year Option)
Cell and Molecular Biology - practicals and tutorials (First Year)
Biological Chemistry - tutorials (First Year)
Research Methods in Biochemistry - practicals (First Year)
Watts, Felicity Z and Hoffmann, Eva (2011) SUMO meets meiosis: an encounter at the synaptonemal complex: SUMO chains and sumoylated proteins suggest that heterogeneous and complex interactions lie at the centre of the synaptonemal complex. BioEssays, 33. pp. 529-33. ISSN 0265-9247
Boyd, L K, Mercer, B, Thompson, D, Main, E and Watts, F Z (2010) Characterisation of the SUMO-like domains of Schizosaccahromyces pombe Rad60. PLoS ONE, 5 (9). e13009. ISSN 1932-6203
Watts, Felicity Z and Brissett, Nigel C (2010) Linking up and interacting with BRCT domains. DNA Repair, 9 (2). pp. 103-8. ISSN 1568-7864
Spirek, Mario, Estreicher, Anna, Csaszar, Edina, Wells, Jennifer, McFarlane, Ramsay J, Watts, Felicity Z and Loidl, Josef (2010) Sumoylation is required for normal development of linear element and wild-type meiotic recombination in Schizosaccharomyces pombe. Chromosoma, 9 (11). pp. 59-72. ISSN 0009-5915
Kilkenny, Mairi L, Doré, Andrew S, Roe, S Mark, Nestoras, Konstantinos, Ho, Jenny C Y, Watts, Felicity Z and Pearl, Laurence H (2008) Structural and functional analysis of the Crb2-BRCT2 domain reveals distinct roles in checkpoint signalling. Genes and Development, 22 (15). pp. 2034-47. ISSN 0890-9369
Watts, F Z, Skilton, A, Ho, J C-Y, Boyd, L K, Trickey, M A M, Gardner, L, Ogi, F-X and Outwin, E A (2007) The role of Schizosaccharomyces pombe SUMO ligases in genome stability. In: Biochemical Society Transactions.
Watts, Felicity (2007) The role of SUMO in chromosome segregation. Chromosoma, 116 (1). pp. 15-20. ISSN 00095915
Watts, Felicity (2006) Sumoylation of PCNA: Wrestling with recombination at stalled replication forks. DNA Repair, 5 (3). pp. 399-403. ISSN 1568-7864
Shin, Jin A, Choi, Eun Shik, Kim, Hyun Soo, Ho, Jenny C Y, Watts, Felicity Z, Park, Sang Dai and Jang, Yeun Kyu (2005) SUMO modification is involved in the maintenance of heterochromatin stability in fission yeast. Molecular Cell, 19 (6). pp. 817-828. ISSN 1097-2765
Watts, Felicity (2004) SUMO modification of proteins other than transcription factors. Seminars in Cell & Developmental Biology, 15 (2). pp. 211-220. ISSN 10849521
