ORCID Profile
0000-0002-2043-5234
Current Organisations
University College London
,
Instituto Gulbenkian de Ciência
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Publisher: American Association for the Advancement of Science (AAAS)
Date: 07-08-2020
Abstract: In eukaryotes, proteasome-mediated degradation of cell cycle factors triggers mitotic exit, DNA segregation, and cytokinesis, a process that culminates in abscission dependent on the protein ESCRT-III. By studying cell ision in an archaeal relative of eukaryotes, Tarrason Risa et al. identified a role for the proteasome in triggering cytokinesis by an archaeal ESCRT-III homolog. Cell ision in this archaeon was driven by stepwise remodeling of a composite ESCRT-III–based ision ring, where rapid proteasome-mediated degradation of one ESCRT-III subunit triggered the constriction of the remaining ESCRT-III–based copolymer. These data strengthen the case for the eukaryotic cell ision machinery having its origins in Archaea. Science , this issue p. eaaz2532
Publisher: The Royal Society
Date: 07-2022
DOI: 10.1098/RSOB.220079
Abstract: Understanding the structure of supramolecular complexes provides insight into their functional capabilities and how they can be modulated in the context of disease. Super-resolution microscopy (SRM) excels in performing this task by resolving ultrastructural details at the nanoscale with molecular specificity. However, technical limitations, such as underlabelling, preclude its ability to provide complete structures. Single-particle analysis (SPA) overcomes this limitation by combining information from multiple images of identical structures and producing an averaged model, effectively enhancing the resolution and coverage of image reconstructions. This review highlights important studies using SRM–SPA, demonstrating how it broadens our knowledge by elucidating features of key biological structures with unprecedented detail.
Publisher: Cold Spring Harbor Laboratory
Date: 08-04-2022
DOI: 10.1101/2022.04.07.487490
Abstract: In recent years, the development of new image analysis approaches has highlighted the possibility of recovering superresolution information from short sequences of wide-field images. Our recently developed method, SRRF (Super-Resolution Radial Fluctuations), enables long-term live-cell imaging beyond the resolution limit without specialized hardware. Here, we present eSRRF (enhanced-SRRF), a significant improvement over our initial method, enhancing image fidelity to the underlying structure and resolution. Especially, eSRRF uses automated data-driven parameter optimization, including an estimation of the number of frames necessary for optimal reconstruction. We demonstrate the improved fidelity of the images reconstructed with eSRRF and highlight its versatility and ease of use over a wide range of microscopy techniques and biological systems. We also extend eSRRF to 3D super-resolution microscopy by combining it with multi-focus microscopy (MFM), obtaining volumetric super-resolution imaging of live cells with acquisition speed of ~1 volume/second.
Publisher: Springer Science and Business Media LLC
Date: 12-08-2016
DOI: 10.1038/NCOMMS12471
Abstract: Despite significant progress, high-speed live-cell super-resolution studies remain limited to specialized optical setups, generally requiring intense phototoxic illumination. Here, we describe a new analytical approach, super-resolution radial fluctuations (SRRF), provided as a fast graphics processing unit-enabled ImageJ plugin. In the most challenging data sets for super-resolution, such as those obtained in low-illumination live-cell imaging with GFP, we show that SRRF is generally capable of achieving resolutions better than 150 nm. Meanwhile, for data sets similar to those obtained in PALM or STORM imaging, SRRF achieves resolutions approaching those of standard single-molecule localization analysis. The broad applicability of SRRF and its performance at low signal-to-noise ratios allows super-resolution using modern widefield, confocal or TIRF microscopes with illumination orders of magnitude lower than methods such as PALM, STORM or STED. We demonstrate this by super-resolution live-cell imaging over timescales ranging from minutes to hours.
Publisher: Springer Science and Business Media LLC
Date: 26-02-2018
DOI: 10.1038/S41598-018-21750-X
Abstract: The bacterial cytoplasmic membrane is the interface between the cell and its environment, with multiple membrane proteins serving its many functions. However, how these proteins are organised to permit optimal physiological processes is largely unknown. Based on our initial findings that 2 phospholipid biosynthetic enzymes (PlsY and CdsA) localise heterogeneously in the membrane of the bacterium Staphylococcus aureus , we have analysed the localisation of other key membrane proteins. A range of protein fusions were constructed and used in conjunction with quantitative image analysis. Enzymes involved in phospholipid biosynthesis as well as the lipid raft marker FloT exhibited a heterogeneous localisation pattern. However, the secretion associated SecY protein, was more homogeneously distributed in the membrane. A FRET-based system also identified novel colocalisation between phospholipid biosynthesis enzymes and the respiratory protein CydB revealing a likely larger network of partners. PlsY localisation was found to be dose dependent but not to be affected by membrane lipid composition. Disruption of the activity of the essential cell ision organiser FtsZ, using the inhibitor PC190723 led to loss of PlsY localisation, revealing a link to cell ision and a possible role for FtsZ in functions not strictly associated with septum formation.
Location: United Kingdom of Great Britain and Northern Ireland
No related grants have been discovered for Ricardo Henriques.