Featured Publications
Structure of the two-component S-layer of the archaeon Sulfolobus acidocaldarius
Lavinia Gambelli, Mathew McLaren, Rebecca Conners, Kelly Sanders, Matthew C Gaines, Lewis Clark, Vicki AM Gold, Daniel Kattnig, Mateusz Sikora, Cyril Hanus, Michail N Isupov, Bertram Daum (2024)
Surface protein layers (S-layers) often form the only structural component of the archaeal cell wall and are therefore important for cell survival. S-layers have a plethora of cellular functions including maintenance of cell shape, osmotic, and mechanical stability, the formation of a semipermeable protective barrier around the cell, and cell–cell interaction, as well as surface adhesion. Despite the central importance of S-layers for archaeal life, their 3-dimensional (3D) architecture is still poorly understood. Here we present the first atomic model of a crenarchaeal S-layer.
CryoEM reveals that ribosomes in microsporidian spores are locked in a dimeric hibernating state
Mathew McLaren, Rebecca Conners, Michail N. Isupov, Patricia Gil-Díez, Lavinia Gambelli, Vicki A. M. Gold, Andreas Walter, Sean R. Connell, Bryony Williams & Bertram Daum (Nature Microbiology 2023)
Using electron cryo-tomography, we investigated how tiny eukaryotic parasites called microsporidia infect animal and human cells. Our research revealed that in dormant microsporidian spores, ribosomes hibernate by forming dimers. Through these findings, we uncovered a potentially fundamental ribosomal "off" switch that governs dormancy across all eukaryotes, such as plant seeds, fungal spores, mammalian egg cells, and quiescent stem cells.
Structure and in situ organisation of the Pyrococcus furiosus archaellum machinery
Bertram Daum, Janet Vonck, Paushali Chaudhury, Robert Reichelt, Sonja-Verena Albers, Reinhard Rachel and Werner Kühlbrandt (2017)
The archaellum is the macromolecular machinery that Archaea use for propulsion or surface adhesion, enabling them to proliferate and invade new territories. The molecular composition of the archaellum and of the motor that drives it appears to be entirely distinct from that of the functionally equivalent bacterial flagellum and flagellar motor. Yet, the structure of the archaellum machinery is scarcely known. Using combined modes of electron cryo-microscopy (cryoEM), we have solved the structure of the Pyrococcus furiosus archaellum filament at 4.2 Å resolution and visualise the architecture and organisation of its motor complex in situ. This allows us to build a structural model combining the archaellum and its motor complex, paving the way to a molecular understanding of archaeal swimming motion
All Publications
CryoEM reveals the structure of an archaeal pilus involved in twitching motility.
Gaines MC, Sivabalasarma S, Isupov MN, Haque R, McLaren M, Hanus C, Gold VAM, Albers SV and Daum B. (2024) Nat. Commun. (accepted)
Archaeal virus entry and egress.
Kuiper BP, Schöntag AMC, Oksanen HM, Daum B, Quax TEF. (2024) µLife
Structure of the two-component S-layer of the archaeon Sulfolobus acidocaldarius.
Gambelli L, McLaren M, Conners R, Sanders K, Gaines MC, Clark L, Gold VAM, Kattnig D, Sikora M, Hanus C, Isupov MN, Daum B (2024)
eLife
The consequence of ATP synthase dimer angle on mitochondrial morphology studied by cryo-electron tomography. Buzzard E, McLaren M, Bragoszewski P, Brancaccio A, Ford H, Daum B, Kuwabara P, Collinson I, Gold V. BiochJ. (2024)
CryoEM reveals that ribosomes in microsporidian spores are locked in a dimeric hibernating state
McLaren M, Conners R, Isupov MN, Gil-Díez P, Gambelli L, Gold VAM, Walter A, Connell SR, Williams B & Daum B (2023)
Nature Microbiology. 8, 1834–1845
doi.org/10.1038/s41564-023-01469-w
Interaction of the periplasmic chaperone Sura with the inner membrane secretion (SEC) machinery. Troman L, Alvira S, Daum B, Gold V, Collison I. BiochJ (2023)
Cryo-electron microscopy of the f1 filamentous phage reveals a new paradigm in viral infection and assembly. Conners R, León-Quezada I, McLaren M, Bennett NJ, Daum B, Rakonjac J, Gold V. Nat. Commun. (2023).
doi:10.1038/s41467-023-37915-w
Electron cryo-microscopy reveals the structure of the archaeal thread filament
Gaines M, Isupov M, Sivabalasarma S, Haque R, McLaren M, Mollat C, Tripp P, Neuhaus A, Gold VAM, Albers SV, Daum B (2022)
Nature Communications. 13, 7411
doi.org/10.1038/s41467-022-34652-4
Escaping the symmetry trap in helical reconstruction
Gambelli L, Isupov MN, Daum B (2022)
Faraday Discussions, 2022
Towards Elucidating the Rotary Mechanism of the Archaellum Machinery
Nuno de Sousa Machado J, Albers SV, Daum B (2022)
Frontiers in Microbiology, volume 13
doi.org/10.3389/fmicb.2022.848597
An archaellum filament composed of two alternating subunits
Gambelli L, Isupov MN, Conners R, McLaren M, Bellack A, Gold VAM, Rachel R and Daum B (2022) Nature Communications, volume 13, Article number: 710
doi.org/10.1038/s41467-022-28337-1
CryoEM structure of the outer membrane secretin channel pIV from the f1 filamentous bacteriophage
Conners R, McLaren M, Łapińska U, Sanders K, Stone MRL, Blaskovich MAT, Pagliara S, Daum B, Rakonjac J & Gold VAM (2021)
Nature Communications volume 12, Article number: 6316
doi.org/10.1038/s41467-021-26610-3
The Polygonal Cell Shape and Surface Protein Layer of Anaerobic Methane-Oxidizing Methylomirabilis lanthanidiphila Bacteria
Gambelli L, Mesman R, Versantvoort W, Diebolder CA, Engel A, Evers W, Jetten MSM, Pabst M, Daum B and van Niftrik L (2021)
Front. Microbiol., 01 December 2021
doi.org/10.3389/fmicb.2021.766527
Inter-membrane association of the Sec and BAM translocons for bacterial outer-membrane biogenesis.
Alvira S, Daniel WW, Troman L, Allen WJ, Lorriman JS, Degliesposti G, Cohen EJ, Beeby M, Daum B, Gold VAM, Skehel JM and Collinson I (2020).
eLife. 2020; 9: e60669. Published online 2020 Nov 4.
Cryo-electron microscopy reveals two distinct type-IV pili assembled by the same bacterium.
Neuhaus A, Muniyandi S, Salzer R, Langer JD, Kruse K, Kirchner L, Sanders K, Daum B, Averhoff B, Gold VAM (2020)
Nat Comm, 2020 May 6;11(1):2231.
doi.org/10.1038/s41467-020-15650-w
Architecture and modular assembly of Sulfolobus S-layers revealed by electron cryotomography.
Gambelli L, Meyer BH, McLaren M, Sanders K, Quax TEF, Gold VAM, Albers SV, Daum B (2019) PNAS 116 (50) 25278-25286.
doi.org/10.1073/pnas.1911262116
Twitch or swim: towards the understanding of prokaryotic motion based on the type IV pilus blueprint.
Daum B, Gold V (2018).
Biological Chemistry 27;399(7):799-808.
Structure and assembly mechanism of virus-associated pyramids.
Quax TEF, Daum B (2018)
Biophysical Reviews 2018 Apr;10(2):551-557. Epub 2017 Dec 4,
doi.org/10.1007/s12551-017-0357-4
Structure and in situ organisation of the Pyrococcus furiosus archaellum machinery.
Daum B, Vonck J, Bellack A, Chaudhury P, Reichelt R, Albers SV, Rachel R, Kühlbrandt W (2017) eLife, 6: e27470.Jun 27.
Supramolecular organization of the human N-BAR domain and its role in shaping the sarcolemma membrane.
Daum B, Auerswald A, Gruber T, Hause G, Balbach J, Kühlbrandt W, Meister A (2016)
Journal of Structural Biology, J Struct Biol 2016 Jun;194(3):375-82. 10.1016/j.jsb.2016.03.017. Epub 2016 Mar 22.
doi.org/10.1016/j.jsb.2016.03.017
S-layers at a second glance? Altiarchaeal grappling hooks (hami) resemble archaeal S-layer proteins in structure and sequence.
Perras A, Daum B, Ziegler C, Takahashi LK, Ahmed M, Wanner G, Klingl G, Leitinger G, Kolb-Lenz D, Gribaldo S, Auerbach A, Mora M, Probst AJ, Bellack A and Moissl-Eichinger C (2015) Frontiers in Microbiology 6:543
doi.org/10.3389/fmicb.2015.00543
Visualization of ATP-synthase dimers in mitochondria by electron cryotomography.
Davies KM, Daum B, Gold V, Mühleip AW, Brandt T, Blum TB, Mills DJ, Kühlbrandt W (2014) Journal of Visualized Experiments, (91):5122,
Self-assembly of the universal membrane-remodeling protein PVAP into 7-fold virus-associated pyramids.
Daum B, Quax TEF, Sachse M, Mills D, Reimann J, Yildiz Ö, Häder S, Saveanu C, Forterre P, Albers SV, Kühlbrandt W and Prangishvili D (2014)
Proceedings of the National Academy of Sciences of the United States of America, 111(10):3829-34,
doi.org/10.1073/pnas.1319245111
First insights into the entry process of hyperthermophilic archaeal viruses.
Quemin ERJ, Lucas S, Daum B, Quax EFT, Kühlbrandt W, Forterre P, Albers SV, Prangishvili D, Krupovic M. (2013)
Journal of Virology 87(24):13379-85,
Age-dependent dissociation of ATP synthase dimers and loss of inner membrane cristae in mitochondria.
Daum B, Walter A, Horst A, Osiewacz H, Kühlbrandt W (2013)
Proceedings of the National Academy of Sciences of the United States of America 111:15301-10
doi.org/10.1073/pnas.1305462110
Role of cryo-ET in membrane bioenergetics research.
Davies KM & Daum B (2013)
Biochemical Society Transactions 41(5):1227-34,
Chloroplast Omp85 proteins change orientation during evolution.
Sommer MS, Daum B, Gross LE, Weis BL, Mirus O, Abram L, Maier UG, Kühlbrandt W, Schleiff E (2011)
Proceedings of the National Academy of Sciences of the United States of America 108: 13841-13846
doi.org/10.1073/pnas.1108626108
Macromolecular organization of ATP synthase and complex I in whole mitochondria.
Davies KM, Strauss M, Daum B, Kief JH, Osiewacz HD, Rycovska A, Zickermann V, Kühlbrandt W (2011)
Proceedings of the National Academy of Sciences of the United States of America 108: 14121-14126
doi.org/10.1073/pnas.1103621108
Electron tomography of plant thylakoid membranes.
Daum B & Kühlbrandt W (2011)
Journal of Experimental Botany 62: 2393-2402
Cyclophilin D links programmed cell death and organismal aging in Podospora anserina.
Brust D, Daum B, Breunig C, Hamann A, Kühlbrandt W, Osiewacz HD (2010)
Aging Cell 9: 761-775
doi.org/10.1111/j.1474-9726.2010.00609.x
Arrangement of photosystem II and ATP synthase in chloroplast membranes of spinach and pea.
Daum B, Nicastro D, Austin J, 2nd, McIntosh JR, Kühlbrandt W (2010)
The Plant Cell 22: 1299-1312