ORCID Profile
0000-0002-2560-6485
Current Organisation
The University of Edinburgh
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Publisher: Cold Spring Harbor Laboratory
Date: 02-07-2023
DOI: 10.1101/2023.07.01.547312
Abstract: Fluorescence microscopy enables specific visualization of proteins in living cells and has played an important role in our understanding of protein subcellular location and function. Some proteins, however, show altered localization and/or function when labeled using direct fusions to fluorescent proteins, making them difficult to study in live cells. Additionally, the resolution of fluorescence microscopy is limited to ∼200 nm, which is two orders of magnitude larger than the size of most proteins. To circumvent these challenges, we previously developed LIVE-PAINT, a live-cell super-resolution approach that takes advantage of short interacting peptides to transiently bind a fluorescent protein to the protein-of-interest. Here, we successfully use LIVE-PAINT to image yeast membrane proteins that do not tolerate the direct fusion of a fluorescent protein by using peptide tags as short as 5-residues. We also demonstrate that it is possible to resolve multiple proteins at the nanoscale concurrently using orthogonal peptide interaction pairs.
Publisher: Wiley
Date: 26-01-2023
DOI: 10.1002/PRO.4558
Abstract: We present direct‐LIVE‐PAINT, an easy‐to‐implement approach for the nanoscopic imaging of protein structures in live cells using labeled binding peptides. We demonstrate the feasibility of direct‐LIVE‐PAINT with an actin‐binding peptide fused to EGFP, the location of which can be accurately determined as it transiently binds to actin filaments. We show that direct‐LIVE‐PAINT can be used to image actin structures below the diffraction‐limit of light and have used it to observe the dynamic nature of actin in live cells. We envisage a similar approach could be applied to imaging other proteins within live mammalian cells.
Publisher: Proceedings of the National Academy of Sciences
Date: 27-05-2014
Abstract: Sterols and triterpenes are complex molecules that are synthesized from the isoprenoid pathway. The functions of sterols in plants have been studied extensively, but the role of triterpenes is less well understood. Here we investigate triterpene synthesis and regulation in diploid oat. We show that the genes for triterpene synthesis are regulated by an ancient root development process that is conserved across erse plants. We further show that mutants in which the metabolism of the most common plant triterpene, β-amyrin, is blocked undergo a change early in the development of the root epidermis that leads to a “superhairy” root phenotype. Our findings shed light on triterpene synthesis and provide evidence for a role for the simple triterpene β-amyrin in plant development.
Publisher: Oxford University Press (OUP)
Date: 03-2013
Abstract: Operon-like gene clusters are an emerging phenomenon in the field of plant natural products. The genes encoding some of the best-characterized plant secondary metabolite biosynthetic pathways are scattered across plant genomes. However, an increasing number of gene clusters encoding the synthesis of erse natural products have recently been reported in plant genomes. These clusters have arisen through the neo-functionalization and relocation of existing genes within the genome, and not by horizontal gene transfer from microbes. The reasons for clustering are not yet clear, although this form of gene organization is likely to facilitate co-inheritance and co-regulation. Oats (Avena spp) synthesize antimicrobial triterpenoids (avenacins) that provide protection against disease. The synthesis of these compounds is encoded by a gene cluster. Here we show that a module of three adjacent genes within the wider biosynthetic gene cluster is required for avenacin acylation. Through the characterization of these genes and their encoded proteins we present a model of the subcellular organization of triterpenoid biosynthesis.
Location: United Kingdom of Great Britain and Northern Ireland
Location: United Kingdom of Great Britain and Northern Ireland
No related grants have been discovered for Susan Rosser.