Specific expression of <i>AtIRT1</i> in phloem companion cells suggests its role in iron translocation in aboveground plant organs

Krausko, Miroslav; Labajová, Mária; Peterková, Darina; Jásik, Ján

doi:10.1080/15592324.2021.1925020

Cited by 6 publications

(4 citation statements)

References 28 publications

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“…AtIRT1, the first ZIP protein identified in Arabidopsis thaliana , is responsible for taking up Zn, Mn, Co, Ni and Cd from the rhizosphere to root cells [ 6 , 7 , 8 , 9 ]. A recent study indicates that AtIRT1 is also specifically expressed in phloem companion cells and has a role in Fe translocation in aboveground organs [ 10 ]. AtIRT2 localizes the vesicle membrane and compartmentalizes Fe into vesicles to prevent its toxicity in the cytosol [ 11 ].…”

Section: Introductionmentioning

confidence: 99%

Genome-Wide Identification and Expression Profile Reveal Potential Roles of Peanut ZIP Family Genes in Zinc/Iron-Deficiency Tolerance

Zhang¹,

Chen²,

Zhang³

et al. 2022

Plants

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Zinc/iron-regulated transporter-like protein (ZIP) family genes play crucial roles in metal uptake and transport in plants. However, little is known about their functions in peanut. Here, genome-wide analysis identified 30 peanut AhZIP genes that were divided into four classes. Most AhZIPs experienced whole-genome or segmental duplication. AhZIP proteins harbored 3–8 transmembrane domains and a typical ZIP domain, showing considerable homology with BbZIP from Bordetella bronchiseptica. Clustered AhZIPs generally share similar gene/protein structures; however, unique features were found in AhIRT1.2, AhZIP1.2, AhZIP3.5 and AhZIP7.8. RNA-seq data revealed that AhZIP2.1/2.2, AhZIP4.1/4.2 and AhZIP11.1/11.2 were highly and preferentially expressed in roots, nodule and reproductive tissues. RT-qPCR analysis indicated that transcriptional responses of AhZIPs to Fe/Zn deficiency are cultivar dependent. The expressions of AhIRT1.1, AhIRT1.2 and AhZIP6.1 were closely related to Fe uptake and translocation. AhIRT1.1 and AhZIP7.2 expression were significantly correlated with Zn accumulation. The expression of AhIRT1.1, AhIRT1.2, AhZIP3.6, AhZIP6.1 and AhZIP11.1 was associated with Mn uptake and translocation. The results confirmed that AhZIP genes play crucial roles in the uptake and transport of Fe, Zn and Mn in peanut, providing clues to further functionally characterize AhZIP genes in the future.

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Section: Introductionmentioning

confidence: 99%

Genome-Wide Identification and Expression Profile Reveal Potential Roles of Peanut ZIP Family Genes in Zinc/Iron-Deficiency Tolerance

Zhang¹,

Chen²,

Zhang³

et al. 2022

Plants

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“…Studies in perennial plants such as Poncirus trifoliata reveal that ZIP members encode proteins with 334 to 419 aa (Fu et al, 2017). Most of the TcZIPs were predicted to be located in the plasma membrane, similarly to AtIRT1, OsZIP4, OsZIP5, HvIRT1 and VvZIP3 (Vert et al, 2002;Ishimaru et al, 2005;Pedas et al, 2008;Lee et al, 2010;Gainza-Corteś et al, 2012;Krausko et al, 2021), and also predicted in the ZIPs members of the Poncirus trifoliata and Zea mays genomes (Li et al, 2013;Fu et al, 2017). However, two TcZIP genes are predicted to be located in the chloroplast.…”

Section: Discussionmentioning

confidence: 99%

Zinc/iron-regulated transporter-like protein gene family in Theobroma cacao L: Characteristics, evolution, function and 3D structure analysis

et al. 2023

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The zinc/iron-regulated transporter-like protein (ZIP) gene family first identified in plants is highly distributed in the plant kingdom. This family has previously been reported to transport several essential and non-essential cationic elements, including those toxic to many economically important crops such as cacao (Theobroma cacao L.). In this article, we present a detailed study on physicochemical properties, evolution, duplication, gene structure, promoter region and TcZIP family three-dimensional protein structure. A total of 11 TcZIP genes have been identified to encode proteins from 309 to 435 aa, with localization in the plasma membrane and chloroplast, containing 6-9 putative domains (TM). Interspecies phylogenetic analysis subdivided the ZIP proteins into four groups. Segmental duplication events significantly contributed to the expansion of TcZIP genes. These genes underwent high pressure of purifying selection. The three-dimensional structure of the proteins showed that α helix conformations are predominant with several pocket sites, containing the metal binding site, with the residues leucine (LEU), alanine (ALA), glycine (GLY), serine (SER), lysine (LYS) and histidine (HIS) the most predicted. Regarding the analysis of the protein-protein interaction and enrichment of the gene ontology, four biological processes were assigned, the most important being the cation transport. These new discoveries expand the knowledge about the function, evolution, protein structures and interaction of ZIP family proteins in cacao and contribute to develop cacao genotypes enriched with important mineral nutrients as well as genotypes that bioaccumulate or exclude toxic metals.

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“…After dewaxing in ethanol, sections were stained with 0.1% basic fuchsine. GUS activity in complex organs of plants grown in the pots was analyzed by histochemistry, also using cryosections as described by Krausko et al. (2021) .…”

Section: Methodsmentioning

confidence: 99%

SYNAPTOTAGMIN 4 is expressed mainly in the phloem and participates in abiotic stress tolerance in Arabidopsis

Kumar,

Krausko,

Jásik

2024

Front. Plant Sci.

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Plant synaptotagmins structurally resemble animal synaptotagmins and extended-synaptotagmins. Animal synaptotagmins are well-characterized calcium sensors in membrane trafficking, and extended-synaptotagmins mediate lipid transfer at the endoplasmic reticulum—plasma membrane contact sites. Here, we characterize SYNAPTOTAGMIN 4 (SYT4), which belongs to the six-member family in Arabidopsis. Fluorometric GUS assay showed that the SYT4 promoter was strongest in roots and the least active in rosettes and cauline leaves, which was confirmed by qPCR. In seedlings, promoter activity was influenced by several factors, such as plant growth regulators, mannitol, sucrose, polyethylene glycol and cold. GUS histochemistry revealed SYT4 promoter activity in the phloem of all organs and even almost exclusively in sieve element precursors and differentiating sieve elements. Accordingly, the SYT-GFP fusion protein also accumulated in these cells with maximal abundance in sieve element precursors. The protein formed a network in the cytoplasm, but during sieve tube differentiation, it deposited at the cell periphery and disappeared from mature tubes. Using photoconvertible fluorescence technology, we showed that a high abundance of SYT4 protein in meristematic protophloem cells was due to its extensive synthesis. SYT4 protein synthesis was interrupted in differentiating sieve elements, but protein degradation was also reduced. In addition to phloem, the fusion protein was detected in shoot and root stem cell niche as early as the late heart stage of the embryo. We isolated and molecularly and biologically characterized five syt4 T-DNA insertion alleles and subjected them to phenotype analysis. The allele with the C2B domain interrupted by an T-DNA insertion exhibits increased sensitivity to factors such as auxins, osmotics, salicylic acid, sodium chloride, and the absence of sucrose in the root growth test.

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Specific expression of AtIRT1 in phloem companion cells suggests its role in iron translocation in aboveground plant organs

Cited by 6 publications

References 28 publications

Genome-Wide Identification and Expression Profile Reveal Potential Roles of Peanut ZIP Family Genes in Zinc/Iron-Deficiency Tolerance

Genome-Wide Identification and Expression Profile Reveal Potential Roles of Peanut ZIP Family Genes in Zinc/Iron-Deficiency Tolerance

Zinc/iron-regulated transporter-like protein gene family in Theobroma cacao L: Characteristics, evolution, function and 3D structure analysis

SYNAPTOTAGMIN 4 is expressed mainly in the phloem and participates in abiotic stress tolerance in Arabidopsis

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