Staff Profile:Professor Simon Andrews

Name:

Professor Simon Andrews

Job Title:

Academic, AMS Building

Responsibilities:

Areas of Interest:

Iron-regulation and virulence in E. coli and Salmonella. Iron is an essential trace element and an important factor in pathogenicity. E. coli and Salmonella possess multiple iron storage and acquisition systems. Our studies are focused on the roles and mechanisms of the iron-storage proteins of these organisms, and their contribution to pathogenicity. áWe have used DNA arrays to identify iron-controlled genes, and are currently investigating the roles of a number of novel potential iron transport systems.

DcuS-DcuR - a two-component sensor-regulator. DcuS-DcuR of E. coli is an interesting two-component sensor-regulator under study in our laboratory. It appears to possess two sensory input domains, one in the periplasm that senses external C4-dicarboxylates (e.g. fumarate and succinate), and another 'PAS' domain in the cytosol that is of unknown function. We are studying the function of the PAS domain, the extent of the DcuSR regulon, and the role of DcuSR in regulating transport. á

Hydrogenase-4. Hydrogenases interconvert H₂ and H⁺ and are used to produce energy in many microorganisms. Our work led to the discovery of a 4th hydrogenase (Hydrogenase-4 or Hyd-4) in E. coli. This enzyme appears to be composed of 10 subunits and multiple metal-containing redox centres. It is encoded by a 12-gene operon (hyfABCDEFGHIJR-focB) that also encodes a sigma54-dependent transcriptional activator (HyfR) and a potential foramate transporter (FocB). Our studies are aimed at determining the function of Hyd-4, and the associated regulator and transporter. á

Functional genomics in E. coli. The E. coli genome contains 4,288 protein-encoding genes of which ~33% (1,400) are of unknown function. We are studying the functions of ~60 highly conserved Unidentified Open-Reading Frames (cURFs) in E. coli through a programme of gene-knockout and phenotypic analysis. Many of these genes are likely to have important and possibly novel functions. á

The di-Mn catalase of Thermus thermophilus. T. thermophilus is a thermophilic bacterium that grows optimally at 60-70^oC. It possesses an unusual di-Mn containing catalase that is highly abundant and appears to be required for normal growth. The structure of the enzyme has been solved at high resolution and we are involved in investigating the structural-functional properties of the enzyme through protein engineering, and we are also interested in further examining redox-stress resistance in T. thermophilus.

Research groups / Centres:

Bacterial Iron Homeostasis

Bacteriology Research in Biomedical Sciences

Publications:

Recent publications:

1. Cornelis, P. and Andrews, S.C. (Editors) 'Iron Uptake and Homeostasis in Microorganisms',June 2010, Pub Caister Academic Press, ISBN: 978-1-904455-65-3
2. Nandal, A., Huggins, C.C.O., Woodhall, M.R., McHugh, J., Rodríguez-Quiñones, F., Quail, M.A., Guest, J.R., and Andrews, S.C. (2010) Induction of the ferritin gene (ftnA) of Escherichia coli by Fe²⁺-Fur is mediated by reversal of H-NS silencing and is RyhB independent. Mol. Microbiol. 75, 637-657.
3. Altonsy, M.O., Andrews, S.C., and Tuohy, K. (2010) Differential induction of apoptosis in human colonic carcinoma cells (Caco-2) by Atopobium, and commensal, probiotic and enteropathogenic bacteria: mediation by the mitochondrial pathway. Int. J. Food Microbiol. (2010) 137, 190-203.
4. Rajasekaran, M.B., Nilapwar, S., Andrews, S.C., and Watson K.A. (2009) EfeO-cupredoxins: major new members of the cupredoxin superfamily with roles in bacterial iron transport. BioMetals DOI: 10.1007/s10534-009-9262-z