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You are here: FRIAS Fellows Fellows 2020/21 Prof. Dr. Conrad W. Mullineaux

Prof. Dr. Conrad W. Mullineaux

University of London
External Senior Fellow
September - December 2014


1982-1985: Undergraduate studies in Natural Sciences, University of Cambridge,UK BA in Natural Sciences (Part II Biochemistry) 2(i); 1985-1988: PhD studies, University of Leeds, UK (Department of Pure and Applied Biology). PhD awarded 1989 "Regulation of photosynthetic excitation energy distribution in cyanobacteria"; 1989-1990: Royal Society Pickering Research Fellow (Max-Planck-Institut für Strahlenchemie, Mülheim an der Ruhr, Germany); 1991-1993: Royal Society Pickering Research Fellow (Robert Hill Institute, Department of Molecular Biology and Biotechnology, University of Sheffield, UK); 1994:University of Sheffield Research Fellow (Robert Hill Institute, Department of Molecular Biology and Biotechnology, University of Sheffield, UK); 1995: Higher Scientific Officer in Biological Spectroscopy, CLRC Daresbury Laboratory, Daresbury, Cheshire, UK; 1995: Visiting scholar, Department of Biochemistry and Molecular Biology, Pennsylvania State University, USA; 1996-2004: Lecturer in Biology (Microbiology) University College London, UK (Senior Lecturer 2000, Reader in Microbiology 2003); since 2005: Professor of Microbiology, Queen Mary, University of London, UK

Current main research interests

  1. Organisation of electron transport chains and regulation of electron transport in Escherichia coli and cyanobacteria.
  2. Organisation, biogenesis and dynamics of photosynthetic membranes in cyanobacteria and plants.
  3. Protein and lipid diffusion in bacterial cells (particularly E. coli and cyanobacteria).
  4. Intercellular communication in multicellular bacteria.
  5. Application of fluorescence microscopy (confocal, FRAP and TIRF) to problems in bacterial cell biology.


Selected Publications

  • Kirchhoff H, Haferkamp S, Allen JF, Epstein DBA, Mullineaux CW (2008) Protein diffusion and macromolecular crowding in thylakoid membranes. Plant Physiol. 146, 1571-1578
  • Lenn T, Leake MC, Mullineaux CW (2008) Clustering and dynamics of cytochrome bd-I complexes in the Escherichia coli plasma membrane in vivo. Mol Microbiol 70, 1397-1407.
  • Mullineaux CW, Mariscal V, Nenninger A, Khanum H, Herrero A, Flores E, Adams DG (2008) Mechanism of intercellular molecular exchange in heterocyst-forming cyanobacteria. EMBO J 27, 1299-1308
  • Goral TK, Johnson MP, Brain APR, Kirchhoff H, Ruban AV, Mullineaux CW (2010) Visualizing the mobility and distribution of chlorophyll-proteins in higher plant thylakoid membranes: effects of photoinhibition and protein phosphorylation Plant Journal 62, 948-959.
  • Liu L-N, Bryan SJ, Huang F, Yu J, Nixon PJ, Rich PR, Mullineaux CW (2012) Control of electron transport routes through redox-regulated redistribution of respiratory complexes. Proc. Natl. Acad. Sci. USA 109, 11431-11436.


FRIAS Research Project

In search of localised membrane protein assembly centres in bacteria

PspA (Phage-Shock Protein A) is a widespread bacterial protein known to be important for preserving membrane integrity under environmental stress conditions. The related Vipp1 protein is found in cyanobacteria (and plant chloroplasts) and seems to play a crucial role in the biogenesis of photosynthetic membranes. In both case, the mechanism of action of the protein is enigmatic. We have visualised both proteins in vivo using fluorescence microscopy and fluorescent protein tags, and found that they form clusters near to the membrane under the conditions when they are likely to be physiologically active. Combined with biochemical identification of interaction partners under these conditions, this suggests a novel hypothesis: that both these proteins may help to organise assembly centres for the rapid and localised production of membrane and secreted proteins. A key prediction of this hypothesis is that specific mRNA molecules should be associated with the PspA and Vipp1 clusters. This project will use the expertise of the Wilde and Hess groups in Biologie III to identify mRNA molecules that may be associated with the protein clusters, using a combination of biochemical approaches (affinity pull-downs and RNA deep-sequencing) with in vivo visualisation of specific mRNAs. In conjunction with the Friedrich group (Biochemie) we will explore the possible role of PspA in biogenesis of respiratory complexes in E. coli.