TY  - JOUR
A1  - Tabatabaei, Iman
A1  - Alseekh, Saleh
A1  - Shahid, Mohammad
A1  - Leniak, Ewa
A1  - Wagner, Mateusz
A1  - Mahmoudi, Henda
A1  - Thushar, Sumitha
A1  - Fernie, Alisdair R.
A1  - Murphy, Kevin M.
A1  - Schmöckel, Sandra M.
A1  - Tester, Mark
A1  - Müller-Röber, Bernd
A1  - Skirycz, Aleksandra
A1  - Balazadeh, Salma
T1  - The diversity of quinoa morphological traits and seed metabolic composition
JF  - Scientific data
N2  - Quinoa (Chenopodium quinoa Willd.) is an herbaceous annual crop of the amaranth family (Amaranthaceae). It is increasingly cultivated for its nutritious grains, which are rich in protein and essential amino acids, lipids, and minerals. Quinoa exhibits a high tolerance towards various abiotic stresses including drought and salinity, which supports its agricultural cultivation under climate change conditions. The use of quinoa grains is compromised by anti-nutritional saponins, a terpenoid class of secondary metabolites deposited in the seed coat; their removal before consumption requires extensive washing, an economically and environmentally unfavorable process; or their accumulation can be reduced through breeding. In this study, we analyzed the seed metabolomes, including amino acids, fatty acids, and saponins, from 471 quinoa cultivars, including two related species, by liquid chromatography - mass spectrometry. Additionally, we determined a large number of agronomic traits including biomass, flowering time, and seed yield. The results revealed considerable diversity between genotypes and provide a knowledge base for future breeding or genome editing of quinoa.
Y1  - 2022
U6  - https://doi.org/10.1038/s41597-022-01399-y
SN  - 2052-4463
VL  - 9
IS  - 1
PB  - Nature Research
CY  - Berlin
ER  - 
TY  - JOUR
A1  - Dortay, Hakan
A1  - Schmöckel, Sandra M.
A1  - Fettke, Jörg
A1  - Müller-Röber, Bernd
T1  - Expression of human c-reactive protein in different systems and its purification from Leishmania tarentolae
JF  - Protein expression and purification
N2  - With its homo-pentameric structure and calcium-dependent specificity for phosphocholine (PCh), human c-reactive protein (CRP) is produced by the liver and secreted in elevated quantities in response to inflammation. CRP is widely accepted as a cardiac marker, e.g. in point-of-care diagnostics, however, its heterologous expression has proven difficult. Here, we demonstrate the expression of CRP in different Escherichia coli strains as well as by in vitro transcription/translation. Although expression in these systems was straightforward, most of the protein that accumulated was insoluble. We therefore expanded our study to include the expression of CRP in two eukaryotic hosts, namely the yeast Kluyveromyces lactis and the protozoon Leishmania tarentolae. Both expression systems are optimized for secretion of recombinant proteins and here allowed successful expression of soluble CRP. We also demonstrate the purification of recombinant CRP from Leishmania growth medium; the purification of protein expressed from K. lactis was not successful. Functional and intact CRP pentamer is known to interact with PCh in Ca(2+)-dependent manner. In this report we verify the binding specificity of recombinant CRP from L tarentolae (2 mu g/mL culture medium) for PCh.
KW  - C-reactive protein
KW  - Protein expression
KW  - Leishmania
KW  - In vitro expression
KW  - Protein purification
Y1  - 2011
U6  - https://doi.org/10.1016/j.pep.2011.03.010
SN  - 1046-5928
VL  - 78
IS  - 1
SP  - 55
EP  - 60
PB  - Elsevier
CY  - San Diego
ER  - 
TY  - JOUR
A1  - Alshareef, Nouf Owdah
A1  - Otterbach, Sophie L.
A1  - Allu, Annapurna Devi
A1  - Woo, Yong H.
A1  - de Werk, Tobias
A1  - Kamranfar, Iman
A1  - Müller-Röber, Bernd
A1  - Tester, Mark
A1  - Balazadeh, Salma
A1  - Schmöckel, Sandra M.
T1  - NAC transcription factors ATAF1 and ANAC055 affect the heat stress response in Arabidopsis
JF  - Scientific reports
N2  - Pre-exposing (priming) plants to mild, non-lethal elevated temperature improves their tolerance to a later higher-temperature stress (triggering stimulus), which is of great ecological importance. 'Thermomemory' is maintaining this tolerance for an extended period of time. NAM/ATAF1/2/ CUC2 (NAC) proteins are plant-specific transcription factors (TFs) that modulate responses to abiotic stresses, including heat stress (HS). Here, we investigated the potential role of NACs for thermomemory. We determined the expression of 104 Ara bidopsis NAC genes after priming and triggering heat stimuli, and found ATAF1 expression is strongly induced right after priming and declines below control levels thereafter during thermorecovery. Knockout mutants of ATAF1 show better thermomemory than wild type, revealing a negative regulatory role. Differential expression analyses of RNA-seq data from ATAF1 overexpressor, ataf1 mutant and wild-type plants after heat priming revealed five genes that might be priming-associated direct targets of ATAF1: AT2G31260 (ATG9), AT2G41640 (GT61), AT3G44990 (XTH31), AT4G27720 and AT3G23540. Based on co-expression analyses applied to the aforementioned RNA-seq profiles, we identified ANAC055 to be transcriptionally co-regulated with ATAF1. Like atafl, anac055 mutants show improved thermomemory, revealing a potential co-control of both NACTFs over thermomemory. Our data reveals a core importance of two NAC transcription factors, ATAF1 and ANAC055, for thermomemory.
Y1  - 2022
U6  - https://doi.org/10.1038/s41598-022-14429-x
SN  - 2045-2322
VL  - 12
IS  - 1
PB  - Nature Research
CY  - Berlin
ER  -