@phdthesis{Siemiatkowska2020,
  author    = {Siemiatkowska, Beata},
  title     = {Redox signalling in plants},
  doi       = {10.25932/publishup-48911},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-489119},
  school      = {Universit{\"a}t Potsdam},
  pages     = {127},
  year      = {2020},
  abstract  = {Once proteins are synthesized, they can additionally be modified by post-translational modifications (PTMs). Proteins containing reactive cysteine thiols, stabilized in their deprotonated form due to their local environment as thiolates (RS-), serve as redox sensors by undergoing a multitude of oxidative PTMs (Ox-PTMs). Ox-PTMs such as S-nitrosylation or formation of inter- or intra-disulfide bridges induce functional changes in these proteins. Proteins containing cysteines, whose thiol oxidation state regulates their functions, belong to the so-called redoxome. Such Ox-PTMs are controlled by site-specific cellular events that play a crucial role in protein regulation, affecting enzyme catalytic sites, ligand binding affinity, protein-protein interactions or protein stability. Reversible protein thiol oxidation is an essential regulatory mechanism of photosynthesis, metabolism, and gene expression in all photosynthetic organisms. Therefore, studying PTMs will remain crucial for understanding plant adaptation to external stimuli like fluctuating light conditions. Optimizing methods suitable for studying plants Ox-PTMs is of high importance for elucidation of the redoxome in plants. This study focusses on thiol modifications occurring in plant and provides novel insight into in vivo redoxome of Arabidopsis thaliana in response to light vs. dark. This was achieved by utilizing a resin-assisted thiol enrichment approach. Furthermore, confirmation of candidates on the single protein level was carried out by a differential labelling approach. The thiols and disulfides were differentially labelled, and the protein levels were detected using immunoblot analysis. Further analysis was focused on light-reduced proteins. By the enrichment approach many well studied redox-regulated proteins were identified. Amongst those were fructose 1,6-bisphosphatase (FBPase) and sedoheptulose-1,7-bisphosphatase (SBPase) which have previously been described as thioredoxin system targeted enzymes. The redox regulated proteins identified in the current study were compared to several published, independent results showing redox regulated proteins in Arabidopsis leaves, root, mitochondria and specifically S-nitrosylated proteins. These proteins were excluded as potential new candidates but remain as a proof-of-concept to the enrichment experiments to be effective. Additionally, CSP41A and CSP41B proteins, which emerged from this study as potential targets of redox-regulation, were analyzed by Ribo-Seq. The active translatome study of csp41a mutant vs. wild-type showed most of the significant changes at end of the night, similarly as csp41b. Yet, in both mutants only several chloroplast-encoded genes were altered. Further studies of CSP41A and CSP41B proteins are needed to reveal their functions and elucidate the role of redox regulation of these proteins.},
  language  = {en}
}
@article{PittarelloGoderisSoensetal.2019,
  author    = {Pittarello, Lidia and Goderis, Steven and Soens, Bastien and McKibbin, Seann J. and Giuli, Gabriele and Bariselli, Federico and Dias, Bruno and Helber, Bernd and Lepore, Giovanni Orazio and Vanhaecke, Frank and K{\"o}berl, Christian and Magin, Thierry E. and Claeys, Philippe},
  title     = {Meteoroid atmospheric entry investigated with plasma flow experiments: Petrography and geochemistry of the recovered material},
  series = {Icarus : international journal of solar system studies},
  volume    = {331},
  journal   = {Icarus : international journal of solar system studies},
  publisher = {Elsevier},
  address   = {San Diego},
  issn      = {0019-1035},
  doi       = {10.1016/j.icarus.2019.04.033},
  pages     = {170 -- 178},
  year      = {2019},
  abstract  = {Melting experiments attempting to reproduce some of the processes affecting asteroidal and cometary material during atmospheric entry have been performed in a high enthalpy facility. For the first time with the specific experimental setup, the resulting material has been recovered, studied, and compared with natural analogues, focusing on the thermal and redox reactions triggered by interaction between the melt and the atmospheric gases under high temperature and low pressure conditions. Experimental conditions were tested across a range of parameters, such as heat flux, experiment duration, and pressure, using two types of sample holders materials, namely cork and graphite. A basalt served as asteroidal analog and to calibrate the experiments, before melting a H5 ordinary chondrite meteorite. The quenched melt recovered after the experiments has been analyzed by mu-XRF, EDS-SEM, EMPA, LA-ICP-MS, and XANES spectroscopy. The glass formed from the basalt is fairly homogeneous, depleted in highly volatile elements (e.g., Na, K), relatively enriched in moderately siderophile elements (e.g., Co, Ni), and has reached an equilibrium redox state with a lower Fe3+/Fe-tot ratio than that in the starting material. Spherical objects, enriched in SiO2, Na2O and K2O, were observed, inferring condensation from the vaporized material. Despite instantaneous quenching, the melt formed from the ordinary chondrite shows extensive crystallization of mostly olivine and magnetite, the latter indicative of oxygen fugacity compatible with presence of both Fe2+ and Fe3+. Similar features have been observed in natural meteorite fusion crusts and in micrometeorites, implying that, at least in terms of maximum temperature reached and chemical reactions, the experiments have successfully reproduced the conditions likely encountered by extraterrestrial material following atmospheric entry.},
  language  = {en}
}