β-Decay Half-Lives of 76;77Co, 79;80Ni, and 81Cu: Experimental Indication of a Doubly Magic 78Ni

published_or_final_versio

Identification of a millisecond isomeric state in 129Cd81 via the detection of internal conversion and Compton electrons

published_or_final_versio

β decay of Cd129 and excited states in In129

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An OregonGreen488-labelled d-amino acid for visualizing peptidoglycan by super-resolution STED nanoscopy

Fluorescent d-amino acids (FDAAs) are molecular probes that are widely used for labelling the peptidoglycan layer of bacteria. When added to growing cells they are incorporated into the stem peptide by a transpeptidase reaction, allowing the timing and localization of peptidoglycan synthesis to be determined by fluorescence microscopy. Herein we describe the chemical synthesis of an OregonGreen488-labelled FDAA (OGDA). We also demonstrate that OGDA can be efficiently incorporated into the PG of Gram-positive and some Gram-negative bacteria, and imaged by super-resolution stimulated emission depletion (STED) nanoscopy at a resolution well below 100 nm.</jats:p

Monopole-Driven Shell Evolution below the Doubly Magic Nucleus Sn132 Explored with the Long-Lived Isomer in Pd126

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New isomers in 125 Pd 79 and 127 Pd 81 : Competing proton and neutron excitations in neutron-rich palladium nuclides towards the N=82 shell closure

The neutron-rich isotopes of palladium have attracted considerable interest in terms of the evolution of the neutron shell closure and its influence on the r-process nucleosynthesis. In this Letter, we present the first spectroscopic information on the excited states in 125Pd79 and 127Pd81 studied using the EURICA γ-ray spectrometer, following production via in-flight fission of a high-intensity 238U beam at the RIBF facility. New isomeric states with half-lives of 144(4) ns and 39(6) μs have been assigned spins and parities of () and () in 125Pd and 127Pd, respectively. The observed level properties are compared to a shell-model calculation, suggesting the competition between proton excitations and neutron excitations in the proton-hole and neutron-hole systems in the vicinity of the doubly magic nucleus 132Sn.Part of the WAS3ABi was supported by the Rare Isotope Science Project which is funded by MSIP and NRF of Korea. This work was supported by the Priority Centers Research Program in Korea (2009-0093817), OTKA contract number K100835, the U.S. DOE, Office of Nuclear Physics (Contract No. DE-AC02-06CH11357), NRF-2016R1A5A1013277 and NRF-2013M7A1A1075764, the Spanish Ministerio de Economía y Competitividad under contract FPA2017-84756-C4-2-P, the European Commission through the Marie Curie Actions call FP7-PEOPLE-2011-IEF (Contract No. 300096), German BMBF under Contract No: 05P12PKFNE, JSPS KAKENHI Grant No. 24740188 and 25247045, the National Natural Science Foundation of China (Nos. 11505302, 11575112), the National Key Program for S&T Research and Development (No. 2016YFA0400501), and STFC (UK)

The bacterial DNA binding protein matp involved in linking the nucleoid terminal domain to the divisome at midcell interacts with lipid membranes

© 2019 Monterroso et al. Division ring formation at midcell is controlled by various mechanisms in Escherichia coli, one of them being the linkage between the chromosomal Ter macrodomain and the Z-ring mediated by MatP, a DNA binding protein that organizes this macrodomain and contributes to the prevention of premature chromosome segregation. Here we show that, during cell division, just before splitting the daughter cells, MatP seems to localize close to the cytoplasmic membrane, suggesting that this protein might interact with lipids. To test this hypothesis, we investigated MatP interaction with lipids in vitro. We found that, when encapsulated inside vesicles and microdroplets generated by microfluidics, MatP accumulates at phospholipid bilayers and monolayers matching the lipid composition in the E. coli inner membrane. MatP binding to lipids was independently confirmed using lipid-coated microbeads and biolayer interferometry assays, which suggested that the recognition is mainly hydrophobic. Interaction of MatP with the lipid membranes also occurs in the presence of the DNA sequences specifically targeted by the protein, but there is no evidence of ternary membrane/protein/DNA complexes. We propose that the association of MatP with lipids may modulate its spatiotemporal localization and its recognition of other ligands. IMPORTANCE The division of an E. coli cell into two daughter cells with equal genomic information and similar size requires duplication and segregation of the chromosome and subsequent scission of the envelope by a protein ring, the Z-ring. MatP is a DNA binding protein that contributes both to the positioning of the Z-ring at midcell and the temporal control of nucleoid segregation. Our integrated in vivo and in vitro analysis provides evidence that MatP can interact with lipid membranes reproducing the phospholipid mixture in the E. coli inner membrane, without concomitant recruitment of the short DNA sequences specifically targeted by MatP. This observation strongly suggests that the membrane may play a role in the regulation of the function and localization of MatP, which could be relevant for the coordination of the two fundamental processes in which this protein participates, nucleoid segregation and cell division