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174 items found (0 items not approved), displaying 1 to 10.[First/Prev] 1, 2, 3, 4, 5, 6, 7, 8 [Next/Last]

Instruments / Technical Area	Publication Details	Published
I18-Microfocus Spectroscopy	Distribution and speciation of Cu and Zn near spring barley (Hordeum vulgare) roots in digested sewage sludge-amended soil Jianting Feng , Ian T. Burke , Felipe E. Sepulveda Olea , Xiaohui Chen , Douglas I. Stewart Environmental Geochemistry And Health 47 DOI: 10.1007/s10653-025-02482-0 Diamond Proposal Number(s): [33049] Open Access Show Abstract ▼ Abstract: Risk management for agricultural use of digested sewage sludge requires better understanding of the behaviour and fate of contaminant metals in the plant root zone. A study employing rhizo-pot and plug-tray experiments was conducted to identify the zone near spring barley roots (Hordeum vulgare) where concentration and speciation of Cu and Zn are affected. Cu and Zn bonding environments in the root epidermis/cortex and vascular tissue were also identified. In the digested sludge-amended soil, spring barley absorbed Cu only from the immediate vicinity of the roots (<< 1 mm), but Zn was taken up from further afield (> 1 mm). In the rhizosphere Cu was predominately present as Cu(I) oxides or as Cu(II) absorbed/bonded to phosphate, whereas Zn was present as Zn(II) in inner-sphere complexes with metal oxide surfaces, as Zn(II) sulphides or Zn(II) bonded to/incorporated into carbonates. Cu taken-up by spring barley roots was largely sequestered in the root epidermis and/or cortex predominately in the coordination environments similar to those seen in the rhizosphere. Only a small proportion of the Cu was translocated into the vascular tissue (where it is in the same two bonding environments). Zn taken-up by spring barley roots was present as Zn(II) sulphides, Zn(II) absorbed to/incorporated into carbonates, or Zn(II)-organic complexes. Zn was readily translocated from roots to shoots. Better understanding of these differences in the mobility and uptake of Cu and Zn in sludge-amended agricultural soils could be used to undertake element specific risk assessments.	May 2025
I04-1-Macromolecular Crystallography (fixed wavelength)	Structural insights into the copper-containing nitrite reductase from Bradyrhizobium japonicum USDA110 and its role in the low nitrite reductase activity of rhizobia Cintia Soledad Ramírez , Carmien Tolmie , María Gabriela Rivas , Pablo Javier Gonzalez , Daniel Horacio Murgida , Diederik J. Opperman , Carlos Dante Brondino , Felix Martin Ferroni Archives Of Biochemistry And Biophysics 4 DOI: 10.1016/j.abb.2025.110467 Diamond Proposal Number(s): [15292] Show Abstract ▼ Abstract: Bradyrhizobium japonicum USDA110 is a widely used microorganism in the formulation of bioinoculants for soybean crops, harboring a copper-containing nitrite reductase with low enzymatic activity. The activity of BjNirK at pH 6.5 was higher compared to that at pH 8.0, regardless of the presence of either physiological or artificial electron donors. Thermal shift assays reveal that the enzyme is more stable at pH 6.5 than at pH 8.0. X-ray structural data reveals that the funnel for substrate entry shows a wider cavity when compared to other class I NirK structures. Furthermore, the presence of an additional channel for proton provision is observed, in addition to the primary and secondary proton channels. The T2Cu active site can accommodate one or two water molecules, resulting in a tetra- or pentacoordinated metal site, respectively. The structural data correlates well with both optical visible and resonance Raman spectroscopies, denoting a strong blue character of the T1Cu site in both solid and solution states. Furthermore, EPR-monitored redox titration reveals that the catalytic rate is not constrained by T1Cu−T2Cu intraprotein electron transfer reaction at either pH 6.5 or pH 8.0. Additionally, bioinformatics studies indicate that the interaction between the enzyme and the electron donor is not pH dependent. These two observations suggest that the low activity of BjNirK is not caused by inefficient donor−enzyme interaction or impaired electron transfer. The present results suggest that the structural architecture and enzyme properties in rhizobia are designed to ensure low activity, a trait that is particularly advantageous for symbiosis.	May 2025
Krios I-Titan Krios I at Diamond Krios III-Titan Krios III at Diamond Krios IV-Titan Krios IV at Diamond	Bacterial pathogen deploys the iminosugar glycosyrin to manipulate plant glycobiology Nattapong Sanguankiattichai , Balakumaran Chandrasekar , Yuewen Sheng , Nathan Hardenbrook , Werner W. A. Tabak , Margit Drapal , Farnusch Kaschani , Clemens Grünwald-Gruber , Daniel Krahn , Pierre Buscaill , Suzuka Yamamoto , Atsushi Kato , Robert Nash , George Fleet , Richard Strasser , Paul D. Fraser , Markus Kaiser , Peijun Zhang , Gail M. Preston , Renier A. L. Van Der Hoorn Science 388, 297 - 303 DOI: 10.1126/science.adp2433 Diamond Proposal Number(s): [21004, 29812, 28713] Show Abstract ▼ Abstract: The extracellular space (apoplast) in plants is a key battleground during microbial infections. To avoid recognition, the bacterial model phytopathogen Pseudomonas syringae pv. tomato DC3000 produces glycosyrin. Glycosyrin inhibits the plant-secreted β-galactosidase BGAL1, which would otherwise initiate the release of immunogenic peptides from bacterial flagellin. Here, we report the structure, biosynthesis, and multifunctional roles of glycosyrin. High-resolution cryo–electron microscopy and chemical synthesis revealed that glycosyrin is an iminosugar with a five-membered pyrrolidine ring and a hydrated aldehyde that mimics monosaccharides. Glycosyrin biosynthesis was controlled by virulence regulators, and its production is common in bacteria and prevents flagellin recognition and alters the extracellular glycoproteome and metabolome of infected plants. These findings highlight a potentially wider role for glycobiology manipulation by plant pathogens across the plant kingdom.	Apr 2025
Krios I-Titan Krios I at Diamond Krios II-Titan Krios II at Diamond	Transport of phenoxyacetic acid herbicides by PIN-FORMED auxin transporters Lukas Schulz , Kien Lam Ung , Lorena Zuzic , Sarah Koutnik-Abele , Birgit Schiøtt , David L. Stokes , Bjørn Panyella Pedersen , Ulrich Z. Hammes Nature Plants 115 DOI: 10.1038/s41477-025-01984-0 Diamond Proposal Number(s): [21404] Open Access Show Abstract ▼ Abstract: Auxins are a group of phytohormones that control plant growth and development. Their crucial role in plant physiology has inspired development of potent synthetic auxins that can be used as herbicides. Phenoxyacetic acid derivatives are a widely used group of auxin herbicides in agriculture and research. Despite their prevalence, the identity of the transporters required for distribution of these herbicides in plants is both poorly understood and the subject of controversial debate. Here we show that PIN-FORMED auxin transporters transport a range of phenoxyacetic acid herbicides across the membrane. We go on to characterize the molecular determinants of substrate specificity using a variety of different substrates as well as protein mutagenesis to probe the binding site. Finally, we present cryogenic electron microscopy structures of Arabidopsis thaliana PIN8 bound to either 2,4-dichlorophenoxyacetic acid or 4-chlorophenoxyacetic acid. These structures represent five key states from the transport cycle, allowing us to describe conformational changes associated with the transport cycle. Overall, our results reveal that phenoxyacetic acid herbicides use the same export machinery as endogenous auxins and exemplify how transporter binding sites undergo transformations that dictate substrate specificity. These results provide a foundation for future development of novel synthetic auxins and for precision breeding of herbicide-resistant crop plants.	Apr 2025
I04-Macromolecular Crystallography I24-Microfocus Macromolecular Crystallography	Comparative analysis of STP6 and STP10 unravels molecular selectivity in sugar transport proteins Camilla Gottlieb Andersen , Laust Bavnhøj , Søren Brag , Anastasiia Bohush , Adriana Chrenkova , Jan Heiner Driller , Bjorn Panyella Pedersen Proceedings Of The National Academy Of Sciences 122 DOI: 10.1073/pnas.2417370122 Diamond Proposal Number(s): [36082, 30015] Show Abstract ▼ Abstract: The distribution of sugars is crucial for plant energy, signaling, and defense mechanisms. Sugar Transport Proteins (STPs) are Sugar Porters (SPs) that mediate proton-driven cellular uptake of glucose. Some STPs also transport fructose, while others remain highly selective for only glucose. What determines this selectivity, allowing STPs to distinguish between compounds with highly similar chemical composition, remains unknown. Here, we present the structure of Arabidopsis thaliana STP6 in an inward-occluded conformational state with glucose bound and demonstrate its role as both a glucose and fructose transporter. We perform a comparative analysis of STP6 with the glucose-selective STP10 using in vivo and in vitro systems, demonstrating how different experimental setups strongly influence kinetic transport properties. We analyze the properties of the monosaccharide binding site and show that the position of a single methyl group in the binding site is sufficient to shuffle glucose and fructose specificity, providing detailed insights into the fine-tuned dynamics of affinity-induced specificity for sugar uptake. Altogether, these findings enhance our understanding of sugar selectivity in STPs and more broadly SP proteins.	Apr 2025
B21-High Throughput SAXS	Iron-sensing and redox properties of the hemerythrin-like domains of Arabidopsis BRUTUS and BRUTUS-LIKE2 proteins Jacob Pullin , Jorge Rodríguez-Celma , Marina Franceschetti , Julia E. A. Mundy , Dimitri A. Svistunenko , Justin M. Bradley , Nick Le Brun , Janneke Balk Nature Communications 16 DOI: 10.1038/s41467-025-58853-9 Diamond Proposal Number(s): [25108] Open Access Show Abstract ▼ Abstract: Iron uptake in plants is negatively regulated by highly conserved hemerythrin (Hr) E3 ubiquitin ligases exemplified by Arabidopsis thaliana BRUTUS (BTS). Physiological studies suggest these are the elusive plant iron sensors, but biochemical evidence is lacking. Here we demonstrate that the N-terminal domains of BTS and BTS-LIKE2 (BTSL2) respectively bind three and two diiron centres within three closely packed Hr-like subdomains. The centres can be reversibly oxidized by O2 and H2O2, resulting in a di-Fe3+ form that is non-labile. In the reduced state, a proportion of the iron becomes labile, based on accessibility to Fe2+ chelators and reconstitution experiments, consistent with dynamic iron binding. Impaired iron binding and altered redox properties in the BTS dgl variant correlate with diminished capacity to suppress the downstream signalling cascade. These data provide the biochemical foundation for a mechanistic model of how BTS/Ls function as iron sensors that are unique to the plant kingdom.	Apr 2025
I04-Macromolecular Crystallography	The Medicago truncatula LYR 4 intracellular domain serves as a scaffold in immunity signaling independent of its phosphorylation activity Bine Simonsen , Henriette Rübsam , Marie Vogel Kolte , Maria Meisner Larsen , Christina Krönauer , Kira Gysel , Mette Laursen , Feng Feng , Gülendam Kaya , Giles E. D. Oldroyd , Jens Stougaard , Sébastien Fort , Simona Radutoiu , Kasper Røjkjær Andersen New Phytologist 118 DOI: 10.1111/nph.70067 Diamond Proposal Number(s): [13062] Open Access Show Abstract ▼ Abstract: In this study, we investigate how the pseudokinase domain of the Medicago LYR4 LysM receptor kinase mediates downstream signaling in immunity. We determine the crystal structure of the LYR4 intracellular domain with an ATP-analog bound in a noncanonical manner and show that it is catalytically active despite its lack of canonical kinase features. However, in planta experiments demonstrate that the phosphorylation ability is not necessary for the function of LYR4 in chitin-triggered ROS production, but that the presence of its intracellular domain is indispensable. Thus, in chitin-triggered immunity the LYR4 intracellular domain serves as a signaling scaffold independent of its catalytic activity.	Mar 2025
	Tethering ferredoxin-NADP+ reductase to photosystem I promotes photosynthetic cyclic electron transfer Thomas Z. Emrich-Mills , Matthew S. Proctor , Gustaf E. Degen , Philip J. Jackson , Katherine H. Richardson , Frederick R. Hawkings , Felix Buchert , Andrew Hitchcock , C. Neil Hunter , Luke C. M. Mackinder , Michael Hippler , Matthew P. Johnson The Plant Cell DOI: 10.1093/plcell/koaf042 Open Access Show Abstract ▼ Abstract: Fixing CO2 via photosynthesis requires ATP and NADPH, which can be generated through linear electron transfer (LET). However, depending on the environmental conditions, additional ATP may be required to fix CO2, which can be generated by cyclic electron transfer (CET). How the balance between LET and CET is determined remains largely unknown. Ferredoxin-NADP+ reductase (FNR) may act as the switch between LET and CET, channelling photosynthetic electrons to LET when it is bound to photosystem I (PSI) or to CET when it is bound to cytochrome b6f. The essential role of FNR in LET precludes the use of a direct gene knock-out to test this hypothesis. Nevertheless, we circumvented this problem using clustered regularly interspaced short palindromic repeats (CRISPR)/CRISPR-associated nuclease 9 (Cas9)-mediated gene editing in Chlamydomonas reinhardtii. Through this approach, we created a chimeric form of FNR tethered to PSI via PSAF. Chimeric FNR mutants exhibited impaired photosynthetic growth and LET along with enhanced PSI acceptor side limitation relative to the wild type due to slower NADPH reduction. However, the chimeric FNR mutants also showed enhanced ΔpH production and NPQ resulting from increased CET. Overall, our results suggest that rather than promoting LET, tethering FNR to PSI promotes CET at the expense of LET and CO2 fixation.	Mar 2025
Krios III-Titan Krios III at Diamond	The structure of the R2T complex reveals a different architecture from the related HSP90 cochaperone R2TP Alberto Palacios-Abella , Andres Lopez-Perrote , Jasminka Boskovic , Sandra Fonseca , Cristina Úrbez , Vicente Rubio , Oscar Llorca , David Alabadí Structure 18 DOI: 10.1016/j.str.2025.01.023 Diamond Proposal Number(s): [26876] Show Abstract ▼ Abstract: The R2TP complex is a specialized HSP90 cochaperone essential for the maturation of macromolecular complexes such as RNAPII and TORC1. R2TP is formed by a hetero-hexameric ring of AAA-ATPases RuvBL1 and RuvBL2, which interact with RPAP3 and PIH1D1. Several R2TP-like complexes have been described, but these are less well characterized. Here, we identified, characterized and determined the cryo-electron microscopy (cryo-EM) structure of R2T from Arabidopsis thaliana, which lacks PIH1D1 and is probably the only form of the complex in seed plants. In contrast to R2TP, R2T is organized as two rings of AtRuvBL1-AtRuvBL2a interacting back-to-back, with one AtRPAP3 anchored per ring. AtRPAP3 has no effect on the ATPase activity of AtRuvBL1-AtRuvBL2a and binds with a different stoichiometry than in human R2TP. We show that the interaction of AtRPAP3 with AtRuvBL2a and AtHSP90 occurs via a conserved mechanism. However, the distinct architectures of R2T and R2TP suggest differences in their functions and mechanisms.	Feb 2025
Krios II-Titan Krios II at Diamond Krios IV-Titan Krios IV at Diamond	Jigsaw puzzle: Deciphering the chloroplast transcription machinery Diamond Light Source Diamond Proposal Number(s): [33824] Show Abstract ▼ Abstract: Chloroplasts are specialised organelles found in plant cells and some algae. Photosynthesis, the process by which light energy is converted into chemical energy, resulting in the production of oxygen and energy-rich organic compounds, takes place in chloroplasts. The number of chloroplasts per plant cell can vary widely, ranging from one in unicellular algae to up to 100 in plants like Arabidopsis and wheat. Chloroplasts have a unique transcription machinery that is more complex than their cyanobacterial ancestors. The plastid-encoded RNA polymerase (PEP) is a multi-subunit complex crucial for transcribing chloroplast genes, which are essential for photosynthesis and plant growth. Despite its importance, the roles of many PEP-associated proteins (PAPs) are poorly understood. Researchers from the John Innes Centre and Diamond Light Source aimed to study the structure of PEP to better understand its composition, assembly, and function. They used cryo-Electron Microscopy (cryo-EM) at the electron Bio Imaging Centre (eBIC) to achieve this goal, providing a detailed view of the PEP complex and its interactions with DNA and RNA. Their work was recently published in Cell.	Jan 2025

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