Dr Julien Bergeron
Tel: 0114 222 2854
We use cryo-Electron Microscopy, combined with X-ray crystallography, NMR and other biophysical methods, to study the structure and mechanism of bacterial nano-machines such as motor complexes, protein delivery systems, etc...
Protein nano-machines are large protein complexes that can perform a mechanical movement upon receiving specific stimuli. In bacteria in particular, these play essential roles in cell organization, motility and interaction with their surroundings. Our goal is to understand the molecular mechanism of action of these nano-machines, and their interaction with other cellular components. Ultimately, we hope to exploit this knowledge for the development of new antibiotics, and of drug delivery systems.
Structural biology, cryo-EM, X-ray crystallography, NMR, nano-machines, bacteriology
Research In Depth
Nano-machines are large protein complexes that can perform a mechanical movement upon receiving specific stimuli. In bacteria in particular, these play essential roles in cell organization, motility and interaction with their surroundings. We are interested in the characterization of these complexes at the atomic level, using a range of stuctural and biophysical methods (cryo-EM, X-ray crystallography, NMR, modelling etc...).
Our goal is to understand the molecular mechanism of action of these nano-machines, and their interaction with other cellular components. Ultimately, we hope to exploit this knowledge for the development of new antibiotics, and of drug delivery systems.
Some of the complexes we are interested in include the bacterial flagellum, the TAD pilus, and the R-body complex.
I welcome applications from prospective home / EU / overseas PhD students and post-doctoral fellows.
• 2017 - Present: Lecturer, Dept. of Molecular Biology and Biotechnology, University of Sheffield
- Kamischke C, Fan J, Bergeron J, Kulasekara H, Dalebroux Z, Burrell A, Kollman J & Miller S (2019) The Acinetobacter baumannii Mla system and glycerophospholipid transport to the outer membrane.. eLife. View this article in WRRO
- Bergeron JRC, Brockerman JA, Vuckovic M, Deng W, Okon M, Finlay BB, McIntosh LP & Strynadka NCJ (2018) Characterization of the two conformations adopted by the T3SS inner-membrane protein PrgK. Protein Science, 27(9), 1680-1691. View this article in WRRO
- Bergeron JRC, Hutto R, Ozyamak E, Hom N, Hansen J, Draper O, Byrne ME, Keyhani S, Komeili A & Kollman JM (2017) Structure of the magnetosome-associated actin-like MamK filament at subnanometer resolution. Protein Science, 26(1), 93-102.
- Worrall LJ, Hong C, Vuckovic M, Deng W, Bergeron JRC, Majewski DD, Huang RK, Spreter T, Finlay BB, Yu Z & Strynadka NCJ (2016) Near-atomic-resolution cryo-EM analysis of the Salmonella T3S injectisome basal body. Nature, 540(7634), 597-601.
- Wong LH, Sinha S, Bergeron JR, Mellor JC, Giaever G, Flaherty P & Nislow C (2016) Reverse Chemical Genetics: Comprehensive Fitness Profiling Reveals the Spectrum of Drug Target Interactions. PLOS Genetics, 12(9). View this article in WRRO
- Bergeron JR (2016) Structural modeling of the flagellum MS ring protein FliF reveals similarities to the type III secretion system and sporulation complex. PeerJ, 4. View this article in WRRO
- Bergeron JRC, Fernández L, Wasney GA, Vuckovic M, Reffuveille F, Hancock REW & Strynadka NCJ (2016) The Structure of a Type 3 Secretion System (T3SS) Ruler Protein Suggests a Molecular Mechanism for Needle Length Sensing. Journal of Biological Chemistry, 291(4), 1676-1691.
- Dicks MDJ, Goujon C, Pollpeter D, Betancor G, Apolonia L, Bergeron JRC & Malim MH (2016) Oligomerization Requirements for MX2-Mediated Suppression of HIV-1 Infection. Journal of Virology, 90(1), 22-32.
- Solomonson M, Setiaputra D, Makepeace KAT, Lameignere E, Petrotchenko EV, Conrady DG, Bergeron JR, Vuckovic M, DiMaio F, Borchers CH , Yip CK et al (2015) Structure of EspB from the ESX-1 Type VII Secretion System and Insights into its Export Mechanism. Structure, 23(3), 571-583.
- Bergeron JRC & Sgourakis NG (2015) Type IV Pilus: One Architectural Problem, Many Structural Solutions. Structure, 23(2), 253-255.
- Bergeron JRC, Worrall LJ, De S, Sgourakis NG, Cheung AH, Lameignere E, Okon M, Wasney GA, Baker D, McIntosh LP & Strynadka NCJ (2015) The Modular Structure of the Inner-Membrane Ring Component PrgK Facilitates Assembly of the Type III Secretion System Basal Body. Structure, 23(1), 161-172.
- Lu Z, Bergeron JRC, Atkinson RA, Schaller T, Veselkov DA, Oregioni A, Yang Y, Matthews SJ, Malim MH & Sanderson MR (2013) Insight into the HIV-1 Vif SOCS-box-ElonginBC interaction. Open Biology, 3(11), 130100-130100.
- Thanabalasuriar A, Bergeron J, Gillingham A, Mimee M, Thomassin J-L, Strynadka N, Kim J & Gruenheid S (2012) Sec24 interaction is essential for localization and virulence-associated function of the bacterial effector protein NleA. Cellular Microbiology, 14(8), 1206-1218.
- Lu D, Fillet S, Meng C, Alguel Y, Kloppsteck P, Bergeron J, Krell T, Gallegos M-T, Ramos J & Zhang X (2010) Crystal structure of TtgV in complex with its DNA operator reveals a general model for cooperative DNA binding of tetrameric gene regulators. Genes & Development, 24(22), 2556-2565.
- Ramboarina S, Garnett JA, Zhou M, Li Y, Peng Z, Taylor JD, Lee W-C, Bodey A, Murray JW, Alguel Y , Bergeron J et al (2010) Structural Insights into Serine-rich Fimbriae from Gram-positive Bacteria. Journal of Biological Chemistry, 285(42), 32446-32457.
- Carpenter EP, Corbett A, Thomson H, Adacha J, Jensen K, Bergeron J, Kasampalidis I, Exley R, Winterbotham M, Tang C , Baldwin GS et al (2007) AP endonuclease paralogues with distinct activities in DNA repair and bacterial pathogenesis. The EMBO Journal, 26(5), 1363-1372.
- Bergeron JRC, Worrall LJ, Sgourakis NG, DiMaio F, Pfuetzner RA, Felise HB, Vuckovic M, Yu AC, Miller SI, Baker D & Strynadka NCJ () A Refined Model of the Prototypical Salmonella SPI-1 T3SS Basal Body Reveals the Molecular Basis for Its Assembly. PLoS Pathogens, 9(4), e1003307-e1003307.
- Sherer NM, Swanson CM, Hué S, Roberts RG, Bergeron JRC & Malim MH () Evolution of a Species-Specific Determinant within Human CRM1 that Regulates the Post-transcriptional Phases of HIV-1 Replication. PLoS Pathogens, 7(11), e1002395-e1002395.
- Autore F, Bergeron JRC, Malim MH, Fraternali F & Huthoff H () Rationalisation of the Differences between APOBEC3G Structures from Crystallography and NMR Studies by Molecular Dynamics Simulations. PLoS ONE, 5(7), e11515-e11515.
- Bergeron JRC, Huthoff H, Veselkov DA, Beavil RL, Simpson PJ, Matthews SJ, Malim MH & Sanderson MR () The SOCS-Box of HIV-1 Vif Interacts with ElonginBC by Induced-Folding to Recruit Its Cul5-Containing Ubiquitin Ligase Complex. PLoS Pathogens, 6(6), e1000925-e1000925.