Imperial College London

DrMorganBeeby

Faculty of Natural SciencesDepartment of Life Sciences

Lecturer in Structural Biology
 
 
 
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Contact

 

+44 (0)20 7594 5251m.beeby Website

 
 
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Location

 

502Sir Ernst Chain BuildingSouth Kensington Campus

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Summary

 

Publications

Publication Type
Year
to

25 results found

Haurat MF, Figueiredo AS, Hoffmann L, Li L, Herr K, J Wilson A, Beeby M, Schaber J, Albers SVet al., 2017, ArnS, a kinase involved in starvation-induced archaellum expression., Mol Microbiol, Vol: 103, Pages: 181-194

Organisms have evolved motility organelles that allow them to move to favourable habitats. Cells integrate environmental stimuli into intracellular signals to motility machineries to direct this migration. Many motility organelles are complex surface appendages that have evolved a tight, hierarchical regulation of expression. In the crenearchaeon Sulfolobus acidocaldarius, biosynthesis of the archaellum is regulated by regulatory network proteins that control expression of archaellum components in a phosphorylation-dependent manner. A major trigger for archaellum expression is nutrient starvation, but although some components are known, the regulatory cascade triggered by starvation is poorly understood. In this work, the starvation-induced Ser/Thr protein kinase ArnS (Saci_1181) which is located proximally to the archaellum operon was identified. Deletion of arnS results in reduced motility, though the archaellum is properly assembled. Therefore, our experimental and modelling results indicate that ArnS plays an essential role in the precisely controlled expression of archaellum components during starvation-induced motility in Sulfolobus acidocaldarius. Furthermore they combined in vivo experiments and mathematical models to describe for the first time in archaea the dynamics of key regulators of archaellum expression.

JOURNAL ARTICLE

Hoffmann L, Schummer A, Reimann J, Haurat MF, Wilson AJ, Beeby M, Warscheid B, Albers SVet al., 2017, Expanding the archaellum regulatory network - the eukaryotic protein kinases ArnC and ArnD influence motility of Sulfolobus acidocaldarius., Microbiologyopen, Vol: 6

Expression of the archaellum, the archaeal-type IV pilus-like rotating motility structure is upregulated under nutrient limitation. This is controlled by a network of regulators, called the archaellum regulatory network (arn). Several of the components of this network in Sulfolobus acidocaldarius can be phosphorylated, and the deletion of the phosphatase PP2A results in strongly increased motility during starvation, indicating a role for phosphorylation in the regulation of motility. Analysis of the motility of different protein kinase deletion strains revealed that deletion of saci_0965, saci_1181, and saci_1193 resulted in reduced motility, whereas the deletion of saci_1694 resulted in hypermotility. Here ArnC (Saci_1193) and ArnD (Saci_1694) are characterized. Purified ArnC and ArnD phosphorylate serine and threonine residues in the C-terminus of the repressor ArnB. arnC is upregulated in starvation medium, whereas arnD is constitutively expressed. However, while differences in the expression and levels of flaB were observed in the ΔarnD strain during growth under rich conditions, under nutrient limiting conditions the ΔarnC and ΔarnD strains showed no large differences in the expression levels of the archaellum or of the studied regulators. This suggests that next to the regulation via the archaellum regulatory network additional regulatory mechanisms of expression and/or activity of the archaellum exist.

JOURNAL ARTICLE

Beeby M, Ribardo DA, Brennan CA, Ruby EG, Jensen GJ, Hendrixson DRet al., 2016, Diverse high-torque bacterial flagellar motors assemble wider stator rings using a conserved protein scaffold, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, Vol: 113, Pages: E1917-E1926, ISSN: 0027-8424

JOURNAL ARTICLE

Nguyen LT, Swulius M, Gumbart JC, Beeby M, Jensen GJet al., 2016, Coarse-Grained Simulations Reveal Mechanisms of Bacterial Morphogenesis, 60th Annual Meeting of the Biophysical-Society, Publisher: CELL PRESS, Pages: 468A-468A, ISSN: 0006-3495

CONFERENCE PAPER

Taylor WR, Matthews-Palmer TRS, Beeby M, 2016, Molecular Models for the Core Components of the Flagellar Type-III Secretion Complex, PLOS ONE, Vol: 11, ISSN: 1932-6203

JOURNAL ARTICLE

Beeby M, 2015, Motility in the epsilon-proteobacteria, CURRENT OPINION IN MICROBIOLOGY, Vol: 28, Pages: 115-121, ISSN: 1369-5274

JOURNAL ARTICLE

Chaban B, Hughes HV, Beeby M, 2015, The flagellum in bacterial pathogens: For motility and a whole lot more, SEMINARS IN CELL & DEVELOPMENTAL BIOLOGY, Vol: 46, Pages: 91-103, ISSN: 1084-9521

JOURNAL ARTICLE

Nguyen LT, Gumbart JC, Beeby M, Jensen GJet al., 2015, Coarse-grained simulations of bacterial cell wall growth reveal that local coordination alone can be sufficient to maintain rod shape, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, Vol: 112, Pages: E3689-E3698, ISSN: 0027-8424

JOURNAL ARTICLE

Beeby M, 2014, Evolution of Novel Components of the Bacterial Flagellar Motor, 28th Annual Symposium of the Protein-Society, Publisher: WILEY-BLACKWELL, Pages: 61-61, ISSN: 0961-8368

CONFERENCE PAPER

Gumbart JC, Beeby M, Jensen GJ, Roux Bet al., 2014, Escherichia coli Peptidoglycan Structure and Mechanics as Predicted by Atomic-Scale Simulations, PLOS COMPUTATIONAL BIOLOGY, Vol: 10, ISSN: 1553-734X

JOURNAL ARTICLE

Mueller A, Beeby M, McDowall AW, Chow J, Jensen GJ, Clemons WMet al., 2014, Ultrastructure and complex polar architecture of the human pathogen Campylobacter jejuni, MICROBIOLOGYOPEN, Vol: 3, Pages: 702-710, ISSN: 2045-8827

JOURNAL ARTICLE

Abrusci P, Vergara-Irigaray M, Johnson S, Beeby MD, Hendrixson DR, Roversi P, Friede ME, Deane JE, Jensen GJ, Tang CM, Lea SMet al., 2013, Architecture of the major component of the type III secretion system export apparatus, NATURE STRUCTURAL & MOLECULAR BIOLOGY, Vol: 20, Pages: 99-U126, ISSN: 1545-9993

JOURNAL ARTICLE

Beeby M, Gumbart JC, Roux B, Jensen GJet al., 2013, Architecture and assembly of the Gram-positive cell wall, MOLECULAR MICROBIOLOGY, Vol: 88, Pages: 664-672, ISSN: 0950-382X

JOURNAL ARTICLE

Jensen G, Briegel A, Beeby M, 2013, Visualizing large macromolecular assemblies in vivo with electron cryotomography, 245th National Spring Meeting of the American-Chemical-Society (ACS), Publisher: AMER CHEMICAL SOC, ISSN: 0065-7727

CONFERENCE PAPER

Beeby M, Cho M, Stubbe J, Jensen GJet al., 2012, Growth and Localization of Polyhydroxybutyrate Granules in Ralstonia eutropha, JOURNAL OF BACTERIOLOGY, Vol: 194, Pages: 1092-1099, ISSN: 0021-9193

JOURNAL ARTICLE

Briegel A, Beeby M, Thanbichler M, Jensen GJet al., 2011, Activated chemoreceptor arrays remain intact and hexagonally packed, MOLECULAR MICROBIOLOGY, Vol: 82, Pages: 748-757, ISSN: 0950-382X

JOURNAL ARTICLE

Chen S, Beeby M, Murphy GE, Leadbetter JR, Hendrixson DR, Briegel A, Li Z, Shi J, Tocheva EI, Mueller A, Dobro MJ, Jensen GJet al., 2011, Structural diversity of bacterial flagellar motors, EMBO JOURNAL, Vol: 30, Pages: 2972-2981, ISSN: 0261-4189

JOURNAL ARTICLE

Chen S, McDowall A, Dobro MJ, Briegel A, Ladinsky M, Shi J, Tocheva EI, Beeby M, Pilhofer M, Ding HJ, Li Z, Gan L, Morris DM, Jensen GJet al., 2010, Electron cryotomography of bacterial cells., J Vis Exp

While much is already known about the basic metabolism of bacterial cells, many fundamental questions are still surprisingly unanswered, including for instance how they generate and maintain specific cell shapes, establish polarity, segregate their genomes, and divide. In order to understand these phenomena, imaging technologies are needed that bridge the resolution gap between fluorescence light microscopy and higher-resolution methods such as X-ray crystallography and NMR spectroscopy. Electron cryotomography (ECT) is an emerging technology that does just this, allowing the ultrastructure of cells to be visualized in a near-native state, in three dimensions (3D), with "macromolecular" resolution (approximately 4nm).(1, 2) In ECT, cells are imaged in a vitreous, "frozen-hydrated" state in a cryo transmission electron microscope (cryoTEM) at low temperature (< -180 degrees C). For slender cells (up to approximately 500 nm in thickness(3)), intact cells are plunge-frozen within media across EM grids in cryogens such as ethane or ethane/propane mixtures. Thicker cells and biofilms can also be imaged in a vitreous state by first "high-pressure freezing" and then, "cryo-sectioning" them. A series of two-dimensional projection images are then collected through the sample as it is incrementally tilted along one or two axes. A three-dimensional reconstruction, or "tomogram" can then be calculated from the images. While ECT requires expensive instrumentation, in recent years, it has been used in a few labs to reveal the structures of various external appendages, the structures of different cell envelopes, the positions and structures of cytoskeletal filaments, and the locations and architectures of large macromolecular assemblies such as flagellar motors, internal compartments and chemoreceptor arrays.(1, 2) In this video article we illustrate how to image cells with ECT, including the processes of sample preparation, dat

JOURNAL ARTICLE

Beeby M, Bobik TA, Yeates TO, 2009, Exploiting genomic patterns to discover new supramolecular protein assemblies, Protein Sci., Vol: 18, Pages: 69-79

JOURNAL ARTICLE

Chim N, McMath LM, Beeby M, Goulding CWet al., 2009, Advances in Mycobacterium tuberculosis structural genomics: investigating potential chinks in the armor of a deadly pathogen, Infect Disord Drug Targets, Vol: 9, Pages: 475-492

JOURNAL ARTICLE

Yeates TO, Beeby M, 2006, Biochemistry. Proteins in a small world, Science, Vol: 314, Pages: 1882-1883

JOURNAL ARTICLE

Beeby M, O Connor BD, Ryttersgaard C, Boutz DR, Perry LJ, Yeates TOet al., 2005, The genomics of disulfide bonding and protein stabilization in thermophiles, PLoS Biol., Vol: 3, Pages: e309-e309

JOURNAL ARTICLE

Kerfeld CA, Sawaya MR, Tanaka S, Nguyen CV, Phillips M, Beeby M, Yeates TOet al., 2005, Protein structures forming the shell of primitive bacterial organelles, Science, Vol: 309, Pages: 936-938

JOURNAL ARTICLE

Strong M, Graeber TG, Beeby M, Pellegrini M, Thompson MJ, Yeates TO, Eisenberg Det al., 2003, Visualization and interpretation of protein networks in Mycobacterium tuberculosis based on hierarchical clustering of genome-wide functional linkage maps, Nucleic Acids Res., Vol: 31, Pages: 7099-7109

JOURNAL ARTICLE

Eads JC, Beeby M, Scapin G, Yu TW, Floss HGet al., 1999, Crystal structure of 3-amino-5-hydroxybenzoic acid (AHBA) synthase, Biochemistry, Vol: 38, Pages: 9840-9849

JOURNAL ARTICLE

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