Dr James Barnett

Senior Lecturer (Biomedical Sciences)

School of Health Sciences

Email:: james.barnett@bcu.ac.uk

James graduated from the University of Sheffield in 2000 with a BSc (Hons) in Biochemistry and Genetics. James’ first graduate job was at The Binding Site Ltd, where he was employed as a technician In the monoclonal antibodies department. James later embarked on a research career, and in 2002 joined the group of Professor Colin Robinson in the Dept of Life Sciences at the University of Warwick. There, James’ research was focused on understanding mechanisms of protein transport in bacteria, and particularly the Tat-pathway.

Following the completion of his PhD in Life Sciences in 2009, James transferred to the Department of Chemistry, and joined Professor Claudia Blindauer’s group as a postdoctoral research fellow. There he investigated the zinc requirements of marine cyanobacteria, using a suite of biochemical and proteomic methods.

In 2014, James took a break from academic research, and spent several years working at Micropathology Ltd, a privately owned biomedical sciences company that specialises in the rapid diagnosis of infectious disease. James developed and validated a number of PCR based tests for the detection of viruses in patient specimens.

James later returned to academia, joining Birmingham City University in 2019, and where he is now a senior lecturer in Biomedical Sciences.

Areas of Expertise

Qualifications

Memberships

Teaching

Research

Postgraduate Supervision

Publications

Barnett JP (2023). Transcriptional response of Burkholderia cenocepacia to severe zinc depletion. British Journal of Biomedical Science 80DOI: 10.3389/bjbs.2023.11597

Coverdale JPC, Barnett JP, Adamu AH, Griffiths EJ, Stewart AJ, and Blindauer CA (2019). A metalloproteomic analysis of interactions between plasma proteins and zinc: elevated fatty acid levels affect zinc distribution. Metallomics 11 1805-1819.

da Costa Paula CA, Gore DM, Shah K, Kuit G, Angunawela RI, Barnett JP, and Tuft SJ (2019). Cytomegalovirus infection is not a major cause of corneal graft failure in the United Kingdom. Eye. 33 833-837.

Pass R, Frudd K, Barnett JP, Blindauer CA, and Brown DR (2015). Prion infection in cells is abolished by a mutated manganese transporter but shows no relation to zinc. Mol Cell Neurosci. 68, 186-193.

Barnett JP, Scanlan DJ, and Blindauer CA (2014). Identification of major zinc-binding proteins from a marine cyanobacterium: insight into metal uptake in oligotrophic environments. Metallomics 6, 1254-1268.

Barnett JP, Blindauer CA, Kassaar O, Khazaipoul S, Martin EM, Sadler PJ, and Stewart AJ (2013). Allosteric modulation of zinc speciation by fatty acids. BBA. 1830 5456-5464.

Van der Ploeg, Monterferrante CG, Piersma S, Barnett JP, Kouwen TRHM, Robinson C, and van Dilj, JM (2012). High salinity growth conditions promote Tat-independent secretion of Tat substrates in Bacillus subtilis. Appl Environ Microbiol 78 7733-7744.

Barnett JP, Millard A, Ksibe A, Scanlan DJ, Schmid R, and Blindauer CA (2012). Mining genomes of cyanobacteria for elements of zinc homeostasis. Front Microbiol Chem. 3, 1-21.

Barnett JP, Scanlan DJ, and Blindauer CA (2012). Protein fractionation and detection for metalloproteomics: challenges and approaches. Anal Bioanal Chem. 402 3311-3322.

Barnett JP, Scanlan DJ, Blindauer CA (2012). Fractionation and identification of metalloproteins from a marine cyanobacterium. Anal Bioanal Chem. 402 3371-3377.

Van der Ploeg R, Barnett JP, Vasisht N, Goosens VJ, Pother DC, Robinson C, and van Dijl JM (2011). Salt Sensitivity of Minimal Twin Arginine Translocases. 286 43759-43770.

Barnett JP, Lawrence J, Mendel S, and Robinson C (2011). Expression of the bifunctional Bacillus subtilis TatAd protein in Escherichia coli reveals distinct TatA/B-family and TatB specific domains. Arch Microbiol. 193, 583-94.

Barnett JP, Robinson C, Scanlan DJ, and Blindauer CA (2011). The Tat protein export pathway and its role in cyanobacterial metalloprotein biosynthesis. FEMS Microbio Lett. 325 1-9.

Barnett JP, van der Ploeg R, Eijlander RT, Nenninger A, Mendel S, Rozeboom R, Kuipers OP, van Dijl JM, and Robinson C (2009). The twin-arginine translocation (Tat) systems from Bacillus subtilis display a conserved mode of complex organization and similar substrate recognition requirements. FEBS J 276, 232-43.

Mendel S., McCarthy A, Barnett JP, Eijlander RT, Nenninger A, Kuipers OP and Robinson C (2008). The Escherichia coli TatABC system and a Bacillus subtilis TatAC-type system recognise three distinct targeting determinants in Twin-arginine signal peptides. J Mol Biol. 375, 661-672.

Barnett JP, Eijlander RT, Kuipers OP, and Robinson C (2008). A minimal Tat system from a Gram-positive organism: a bifunctional TatA subunit participates in discrete TatAC and TatA complexes. J Biol Chem. 283, 2534-42.

Oates J, Barrett CML, Barnett JP, Byrne KG, Bolhuis A, and Robinson C (2005). The Escherichia coli Twin-arginine Translocation Apparatus Incorporates a Distinct Form of TatABC Complex, Spectrum of Modular TatA Complexes and Minor TatAB Complex. J Mol Biol. 346 295-305.