TY - GEN A1 - Higgs, Eric S. A1 - Harris, Jim A. A1 - Heger, Tina A1 - Hobbs, Richard J. A1 - Murphy, Stephen D. A1 - Suding, Katharine N. T1 - Keep ecological restoration open and flexible T2 - Nature Ecology & Evolution Y1 - 2018 U6 - https://doi.org/10.1038/s41559-018-0483-9 SN - 2397-334X VL - 2 IS - 4 SP - 580 EP - 580 PB - Nature Publ. Group CY - London ER - TY - GEN A1 - Kramer, Elena M. A1 - Lenhard, Michael T1 - Shape and form in plant development T2 - Seminars in cell & developmental biology Y1 - 2017 U6 - https://doi.org/10.1016/j.semcdb.2017.11.004 SN - 1084-9521 VL - 79 SP - 1 EP - 2 PB - Elsevier CY - London ER - TY - GEN A1 - Best, Robert B. A1 - Zheng, Wenwei A1 - Borgia, Alessandro A1 - Buholzer, Karin A1 - Borgia, Madeleine B. A1 - Hofmann, Hagen A1 - Soranno, Andrea A1 - Nettels, Daniel A1 - Gast, Klaus A1 - Grishaev, Alexander A1 - Schuler, Benjamin T1 - Comment on "Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water" T2 - Science N2 - Riback et al. (Reports, 13 October 2017, p. 238) used small-angle x-ray scattering (SAXS) experiments to infer a degree of compaction for unfolded proteins in water versus chemical denaturant that is highly consistent with the results from Forster resonance energy transfer (FRET) experiments. There is thus no "contradiction" between the two methods, nor evidence to support their claim that commonly used FRET fluorophores cause protein compaction. Y1 - 2018 U6 - https://doi.org/10.1126/science.aar7101 SN - 0036-8075 SN - 1095-9203 VL - 361 IS - 6405 PB - American Assoc. for the Advancement of Science CY - Washington ER - TY - GEN A1 - Sicard, Adrien A1 - Lenhard, Michael T1 - Capsella T2 - Current biology Y1 - 2018 U6 - https://doi.org/10.1016/j.cub.2018.06.033 SN - 0960-9822 SN - 1879-0445 VL - 28 IS - 17 SP - R920 EP - R921 PB - Cell Press CY - Cambridge ER - TY - GEN A1 - Albers, Philip A1 - Uestuen, Suayib A1 - Witzel, Katja A1 - Bornke, Frederik T1 - Identification of a novel target of the bacterial effector HopZ1a T2 - Phytopathology N2 - The plant pathogen Pseudomonas syringae is a gram-negative bacterium which infects a wide range of plant species including important crops plants. To suppress plant immunity and cause disease P.syringae injects type-III effector proteins (T3Es) into the plant cell cytosol. In this study, we identified a novel target of the well characterized bacterial T3E HopZ1a. HopZ1a is an acetyltransferase that was shown to disrupt vesicle transport during innate immunity by acetylating tubulin. Using a yeast-two-hybrid screen approach, we identified a REMORIN (REM) protein from tobacco as a novel HopZ1a target. HopZ1a interacts with REM at the plasma membrane (PM) as shown by split-YFP experiments. Interestingly, we found that PBS1, a well-known kinase involved in plant immunity also interacts with REM in pull-down assays, and at the PM as shown by BiFC. Furthermore, we confirmed that REM is phosphorylated by PBS1 in vitro. Overexpression of REM provokes the upregulation of defense genes and leads to disease-like phenotypes pointing to a role of REM in plant immune signaling. Further protein-protein interaction studies reveal novel REM binding partners with a possible role in plant immune signaling. Thus, REM might act as an assembly hub for an immune signaling complex targeted by HopZ1a. Taken together, this is the first report describing that a REM protein is targeted by a bacterial effector. How HopZ1a might mechanistically manipulate the plant immune system through interfering with REM function will be discussed. Y1 - 2018 SN - 0031-949X SN - 1943-7684 VL - 108 IS - 10 PB - American Phytopathological Society CY - Saint Paul ER - TY - GEN A1 - Messerschmidt, Katrin A1 - Machens, Fabian A1 - Hochrein, Lena A1 - Naseri, Gita T1 - Orthogonal, light-inducible protein expression platform in yeast Sacchararomyces cerevisiae T2 - New biotechnology Y1 - 2018 U6 - https://doi.org/10.1016/j.nbt.2018.05.153 SN - 1871-6784 SN - 1876-4347 VL - 44 SP - S19 EP - S19 PB - Elsevier CY - Amsterdam ER - TY - GEN A1 - Gräf, Ralph T1 - Comparative Biology of Centrosomal Structures in Eukaryotes T2 - Cells N2 - The centrosome is not only the largest and most sophisticated protein complex within a eukaryotic cell, in the light of evolution, it is also one of its most ancient organelles. This special issue of "Cells" features representatives of three main, structurally divergent centrosome types, i.e., centriole-containing centrosomes, yeast spindle pole bodies (SPBs), and amoebozoan nucleus-associated bodies (NABs). Here, I discuss their evolution and their key-functions in microtubule organization, mitosis, and cytokinesis. Furthermore, I provide a brief history of centrosome research and highlight recently emerged topics, such as the role of centrioles in ciliogenesis, the relationship of centrosomes and centriolar satellites, the integration of centrosomal structures into the nuclear envelope and the involvement of centrosomal components in non-centrosomal microtubule organization. KW - centrosome KW - centriole KW - cilium KW - basal body KW - spindle pole body KW - SPB KW - nucleus-associated body KW - NAB KW - microtubules Y1 - 2018 U6 - https://doi.org/10.3390/cells7110202 SN - 2073-4409 VL - 7 IS - 11 PB - MDPI CY - Basel ER - TY - GEN A1 - Balazadeh, Salma A1 - Müller-Röber, Bernd T1 - A balance to death T2 - Nature plants N2 - Leaf senescence plays a crucial role in nutrient recovery in late-stage plant development and requires vast transcriptional reprogramming by transcription factors such as ORESARA1 (ORE1). A proteolytic mechanism is now found to control ORE1 degradation, and thus senescence, during nitrogen starvation. Y1 - 2018 U6 - https://doi.org/10.1038/s41477-018-0279-6 SN - 2055-026X SN - 2055-0278 VL - 4 IS - 11 SP - 863 EP - 864 PB - Nature Publ. Group CY - London ER - TY - GEN A1 - Barlow, Axel A1 - Sheng, Gui-Lian A1 - Lai, Xu-Long A1 - Hofreiter, Michael A1 - Paijmans, Johanna L. A. T1 - Once lost, twice found: Combined analysis of ancient giant panda sequences characterises extinct clade T2 - Journal of biogeography Y1 - 2018 U6 - https://doi.org/10.1111/jbi.13486 SN - 0305-0270 SN - 1365-2699 VL - 46 IS - 1 SP - 251 EP - 253 PB - Wiley CY - Hoboken ER - TY - GEN A1 - Dierschke, Hartmut A1 - Heinken, Thilo T1 - Vorwort T2 - Tuexenia : Mitteilungen der Floristisch-Soziologischen Arbeitsgemeinschaft Y1 - 2019 UR - https://www.tuexenia.de/publications/tuexenia/Tuexenia_2019_NS_039_0007-0007.pdf SN - 0722-494X IS - 39 SP - 7 EP - 7 PB - Floristisch-Soziologische Arbeitsgemeinschaft CY - Göttingen ER - TY - GEN A1 - Hermanussen, Michael A1 - Scheffler, Christiane A1 - Groth, Detlef A1 - Bogin, Barry T1 - Student work on trends in infant and child growth BT - an editorial T2 - Journal of biological and clinical anthropology : Anthropologischer Anzeiger : Mitteilungsorgan der Gesellschaft für Anthropologie KW - nutrition KW - impact on growth KW - geographic neighborhood KW - mortality bias KW - limb disproportions KW - physical activity KW - socioeconomic status KW - parental age KW - statistical tools Y1 - 2019 U6 - https://doi.org/10.1127/anthranz/2019/1052 SN - 0003-5548 VL - 76 IS - 5 SP - 363 EP - 364 PB - Schweizerbart CY - Stuttgart ER - TY - GEN A1 - de Vera, Jean-Pierre Paul A1 - Alawi, Mashal A1 - Backhaus, Theresa A1 - Baque, Mickael A1 - Billi, Daniela A1 - Boettger, Ute A1 - Berger, Thomas A1 - Bohmeier, Maria A1 - Cockell, Charles A1 - Demets, Rene A1 - de la Torre Noetzel, Rosa A1 - Edwards, Howell A1 - Elsaesser, Andreas A1 - Fagliarone, Claudia A1 - Fiedler, Annelie A1 - Foing, Bernard A1 - Foucher, Frederic A1 - Fritz, Jörg A1 - Hanke, Franziska A1 - Herzog, Thomas A1 - Horneck, Gerda A1 - Hübers, Heinz-Wilhelm A1 - Huwe, Björn A1 - Joshi, Jasmin Radha A1 - Kozyrovska, Natalia A1 - Kruchten, Martha A1 - Lasch, Peter A1 - Lee, Natuschka A1 - Leuko, Stefan A1 - Leya, Thomas A1 - Lorek, Andreas A1 - Martinez-Frias, Jesus A1 - Meessen, Joachim A1 - Moritz, Sophie A1 - Moeller, Ralf A1 - Olsson-Francis, Karen A1 - Onofri, Silvano A1 - Ott, Sieglinde A1 - Pacelli, Claudia A1 - Podolich, Olga A1 - Rabbow, Elke A1 - Reitz, Günther A1 - Rettberg, Petra A1 - Reva, Oleg A1 - Rothschild, Lynn A1 - Garcia Sancho, Leo A1 - Schulze-Makuch, Dirk A1 - Selbmann, Laura A1 - Serrano, Paloma A1 - Szewzyk, Ulrich A1 - Verseux, Cyprien A1 - Wadsworth, Jennifer A1 - Wagner, Dirk A1 - Westall, Frances A1 - Wolter, David A1 - Zucconi, Laura T1 - Limits of life and the habitability of Mars BT - the ESA space experiment BIOMEX on the ISS T2 - Astrobiology N2 - BIOMEX (BIOlogy and Mars EXperiment) is an ESA/Roscosmos space exposure experiment housed within the exposure facility EXPOSE-R2 outside the Zvezda module on the International Space Station (ISS). The design of the multiuser facility supports-among others-the BIOMEX investigations into the stability and level of degradation of space-exposed biosignatures such as pigments, secondary metabolites, and cell surfaces in contact with a terrestrial and Mars analog mineral environment. In parallel, analysis on the viability of the investigated organisms has provided relevant data for evaluation of the habitability of Mars, for the limits of life, and for the likelihood of an interplanetary transfer of life (theory of lithopanspermia). In this project, lichens, archaea, bacteria, cyanobacteria, snow/permafrost algae, meristematic black fungi, and bryophytes from alpine and polar habitats were embedded, grown, and cultured on a mixture of martian and lunar regolith analogs or other terrestrial minerals. The organisms and regolith analogs and terrestrial mineral mixtures were then exposed to space and to simulated Mars-like conditions by way of the EXPOSE-R2 facility. In this special issue, we present the first set of data obtained in reference to our investigation into the habitability of Mars and limits of life. This project was initiated and implemented by the BIOMEX group, an international and interdisciplinary consortium of 30 institutes in 12 countries on 3 continents. Preflight tests for sample selection, results from ground-based simulation experiments, and the space experiments themselves are presented and include a complete overview of the scientific processes required for this space experiment and postflight analysis. The presented BIOMEX concept could be scaled up to future exposure experiments on the Moon and will serve as a pretest in low Earth orbit. KW - EXPOSE-R2 KW - BIOMEX KW - Habitability KW - Limits of life KW - Extremophiles KW - Mars Y1 - 2019 U6 - https://doi.org/10.1089/ast.2018.1897 SN - 1531-1074 SN - 1557-8070 VL - 19 IS - 2 SP - 145 EP - 157 PB - Liebert CY - New Rochelle ER - TY - GEN A1 - Sowemimo, Oluwakemi A1 - Borcherds, Wade A1 - Knox-Brown, Patrick A1 - Rindfleisch, Tobias A1 - Thalhammer, Anja A1 - Daughdrill, Gary T1 - Evolution of Transient Helicity and Disorder in Late Embryogenesis Abundant Protein COR15A T2 - Biophysical journal N2 - Cold regulated protein 15A (COR15A) is a nuclear encoded, intrinsically disordered protein that is found in Arabidopsis thaliana. It belongs to the Late Embryogenesis Abundant (LEA) family of proteins and is responsible for increased freezing tolerance in plants. COR15A is intrinsically disordered in dilute solutions and adopts a helical structure upon dehydration or in the presence of co-solutes such as TFE and ethylene glycol. This helical structure is thought to be important for protecting plants from dehydration induced by freezing. Multiple protein sequence alignments revealed the presence of several conserved glycine residues that we hypothesize keeps COR15A from becoming helical in dilute solutions. Using AGADIR, the change in helical content of COR15A when these conserved glycine residues were mutated to alanine residues was predicted. Based on the predictions, glycine to alanine mutants were made at position 68, and 54,68,81, and 84. Labeled samples of wildtype COR15A and mutant proteins were purified and NMR experiments were performed to examine any structural changes induced by the mutations. To test the effects of dehydration on the structure of COR15A, trifluoroethanol, an alcohol based co solvent that is proposed to induce/stabilize helical structure in peptides was added to the NMR samples, and the results of the experiment showed an increase in helical content, compared to the samples without TFE. To test the functional differences between wild type and the mutants, liposome leakage assays were performed. The results from these assays suggest the more helical mutants may augment membrane stability. Y1 - 2019 U6 - https://doi.org/10.1016/j.bpj.2018.11.2553 SN - 0006-3495 SN - 1542-0086 VL - 116 IS - 3 SP - 473A EP - 473A PB - Cell Press CY - Cambridge ER - TY - GEN A1 - Arnold, Patrick T1 - The origin of morphological integration and modularity in the Mammalian Neck T2 - Journal of morphology Y1 - 2019 U6 - https://doi.org/10.1002/jmor.21003 SN - 0362-2525 SN - 1097-4687 VL - 280 SP - S13 EP - S13 PB - Wiley CY - Hoboken ER - TY - GEN A1 - Radchuk, Viktoriia A1 - Kramer-Schadt, Stephanie A1 - Grimm, Volker T1 - Transferability of mechanistic ecological models is about emergence T2 - Trends in ecology and evolution Y1 - 2019 U6 - https://doi.org/10.1016/j.tree.2019.01.010 SN - 0169-5347 SN - 1872-8383 VL - 34 IS - 6 SP - 487 EP - 488 PB - Elsevier CY - London ER - TY - GEN A1 - Numberger, Daniela A1 - Dreier, Carola A1 - Vullioud, Colin A1 - Gabriel, Guelsah A1 - Greenwood, Alex D. A1 - Grossart, Hans-Peter T1 - Correction: Recovery of influenza A viruses from lake water and sediments by experimental inoculation (vol 14, e0216880, 2019) T2 - PLoS one Y1 - 2019 U6 - https://doi.org/10.1371/journal.pone.0218882 SN - 1932-6203 VL - 14 IS - 6 PB - PLoS CY - San Fransisco ER - TY - GEN A1 - Moga, A. A1 - Robinson, T. A1 - Leimkühler, Silke T1 - Towards reconstituting a biosynthetic pathway within compartmentalized GUVs T2 - European biophysics journal : with biophysics letters ; an international journal of biophysics Y1 - 2019 SN - 0175-7571 SN - 1432-1017 VL - 48 SP - S218 EP - S218 PB - Springer CY - New York ER - TY - GEN A1 - Luckner, Madlen A1 - Dunsing, Valentin A1 - Drüke, Markus A1 - Zuehlke, B. A1 - Petazzi, Roberto Arturo A1 - Chiantia, Salvatore A1 - Herrmann, A. T1 - Quantifying protein oligomerization directly in living cells BT - a systematic comparison of fluorescent proteins and application to Influenza A virus infection T2 - European biophysics journal : with biophysics letters ; an international journal of biophysics Y1 - 2019 SN - 0175-7571 SN - 1432-1017 VL - 48 SP - S183 EP - S183 PB - Springer CY - New York ER - TY - GEN A1 - Dunsing, Valentin A1 - Irmscher, Tobias A1 - Barbirz, Stefanie A1 - Chiantia, Salvatore T1 - Microviscosity of bacterial biofilm matrix characterized by fluorescence correlation spectroscopy and single particle tracking T2 - European biophysics journal : with biophysics letters ; an international journal of biophysics Y1 - 2019 U6 - https://doi.org/https://doi.org/10.1007/s00249-019-01373-4 SN - 0175-7571 SN - 1432-1017 VL - 48 SP - S115 EP - S115 PB - Springer CY - New York ER - TY - GEN A1 - Rodriguez-Sillke, Yasmina A1 - Steinhoff, U. A1 - Bojarski, Christian A1 - Lissner, Donata A1 - Schumann, Michael A1 - Branchi, F. A1 - Siegmund, Britta A1 - Glauben, Rainer T1 - Deep immune profiling of human Peyer´s Patches in patients of inflammatory bowel diseases T2 - European journal of immunology Y1 - 2019 U6 - https://doi.org/10.1002/eji.201970300 SN - 0014-2980 SN - 1521-4141 VL - 49 SP - 203 EP - 204 PB - Wiley CY - Weinheim ER -