TY  - JOUR
A1  - Bazihizina, Nadia
A1  - Böhm, Jennifer
A1  - Messerer, Maxim
A1  - Stigloher, Christian
A1  - Müller, Heike M.
A1  - Cuin, Tracey Ann
A1  - Maierhofer, Tobias
A1  - Cabot, Joan
A1  - Mayer, Klaus F. X.
A1  - Fella, Christian
A1  - Huang, Shouguang
A1  - Al‐Rasheid, Khaled A. S.
A1  - Alquraishi, Saleh
A1  - Breadmore, Michael
A1  - Mancuso, Stefano
A1  - Shabala, Sergey
A1  - Ache, Peter
A1  - Zhang, Heng
A1  - Zhu, Jian‐Kang
A1  - Hedrich, Rainer
A1  - Scherzer, Sönke
T1  - Stalk cell polar ion transport provide for bladder‐based salinity tolerance in Chenopodium quinoa
JF  - New Phytologist
N2  - Chenopodium quinoa uses epidermal bladder cells (EBCs) to sequester excess salt. Each EBC complex consists of a leaf epidermal cell, a stalk cell, and the bladder.

Under salt stress, sodium (Na\(^{+}\)), chloride (Cl\(^{−}\)), potassium (K\(^{+}\)) and various metabolites are shuttled from the leaf lamina to the bladders. Stalk cells operate as both a selectivity filter and a flux controller.

In line with the nature of a transfer cell, advanced transmission electron tomography, electrophysiology, and fluorescent tracer flux studies revealed the stalk cell’s polar organization and bladder‐directed solute flow.

RNA sequencing and cluster analysis revealed the gene expression profiles of the stalk cells. Among the stalk cell enriched genes, ion channels and carriers as well as sugar transporters were most pronounced. Based on their electrophysiological fingerprint and thermodynamic considerations, a model for stalk cell transcellular transport was derived.
KW  - halophyte
KW  - polar ion transport
KW  - quinoa
KW  - salt tolerance
KW  - stalk cell
Y1  - 2022
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-287222
VL  - 235
IS  - 5
SP  - 1822
EP  - 1835
ER  - 
TY  - JOUR
A1  - Rasouli, Fatemeh
A1  - Kiani-Pouya, Ali
A1  - Shabala, Lana
A1  - Li, Leiting
A1  - Tahir, Ayesha
A1  - Yu, Min
A1  - Hedrich, Rainer
A1  - Chen, Zhonghua
A1  - Wilson, Richard
A1  - Zhang, Heng
A1  - Shabala, Sergey
T1  - Salinity effects on guard cell proteome in Chenopodium quinoa
JF  - International Journal of Molecular Sciences
N2  - Epidermal fragments enriched in guard cells (GCs) were isolated from the halophyte quinoa (Chenopodium quinoa Wild.) species, and the response at the proteome level was studied after salinity treatment of 300 mM NaCl for 3 weeks. In total, 2147 proteins were identified, of which 36% were differentially expressed in response to salinity stress in GCs. Up and downregulated proteins included signaling molecules, enzyme modulators, transcription factors and oxidoreductases. The most abundant proteins induced by salt treatment were desiccation-responsive protein 29B (50-fold), osmotin-like protein OSML13 (13-fold), polycystin-1, lipoxygenase, alpha-toxin, and triacylglycerol lipase (PLAT) domain-containing protein 3-like (eight-fold), and dehydrin early responsive to dehydration (ERD14) (eight-fold). Ten proteins related to the gene ontology term “response to ABA” were upregulated in quinoa GC; this included aspartic protease, phospholipase D and plastid-lipid-associated protein. Additionally, seven proteins in the sucrose–starch pathway were upregulated in the GC in response to salinity stress, and accumulation of tryptophan synthase and L-methionine synthase (enzymes involved in the amino acid biosynthesis) was observed. Exogenous application of sucrose and tryptophan, L-methionine resulted in reduction in stomatal aperture and conductance, which could be advantageous for plants under salt stress. Eight aspartic proteinase proteins were highly upregulated in GCs of quinoa, and exogenous application of pepstatin A (an inhibitor of aspartic proteinase) was accompanied by higher oxidative stress and extremely low stomatal aperture and conductance, suggesting a possible role of aspartic proteinase in mitigating oxidative stress induced by saline conditions.
KW  - quinoa
KW  - guard cell
KW  - stomata
KW  - salt stress
KW  - proteomics analysis
Y1  - 2021
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-285625
SN  - 1422-0067
VL  - 22
IS  - 1
ER  -