Molecular Mechanism of Nramp-Family Transition Metal Transport

Bozzi, Aaron T.; Gaudet, Rachelle

doi:10.1016/j.jmb.2021.166991

Cited by 59 publications

(76 citation statements)

References 208 publications

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“…For reversal-potential assays, it is generally assumed that the transport reaction is reversible and thus, that protein orientation does not matter. However, this assumption does not always hold, as has recently been demonstrated with the proton-coupled metal symporter DraNramp ( 15 , 43 , 44 ). Transporter orientation was addressed in two ways in our assays.…”

Section: Discussionmentioning

confidence: 99%

A solid-supported membrane electrophysiology assay for efficient characterization of ion-coupled transport

Thomas

Feng

Henzler‐Wildman

2021

Journal of Biological Chemistry

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This is a PDF file of an article that has undergone enhancements after acceptance, such as the addition of a cover page and metadata, and formatting for readability, but it is not yet the definitive version of record. This version will undergo additional copyediting, typesetting and review before it is published in its final form, but we are providing this version to give early visibility of the article. Please note that, during the production process, errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain.

show abstract

Section: Discussionmentioning

confidence: 99%

A solid-supported membrane electrophysiology assay for efficient characterization of ion-coupled transport

Thomas

Feng

Henzler‐Wildman

2021

Journal of Biological Chemistry

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“…NRAMP proteins function as divalent metal transporters in a wide range of living beings from bacteria to humans (Bozzi & Gaudet, 2021). A large number of NRAMP proteins of different species have been reported as metal ion transporters mediating multiple‐element transportation.…”

Section: Discussionmentioning

confidence: 99%

“…The natural resistance‐associated macrophage proteins (NRAMPs) play important roles in the uptake, transportation and detoxification of multiple metal ions in a wide range of living beings from bacteria to humans (Bozzi & Gaudet, 2021). Rice genome encodes seven NRAMP proteins (Mani & Sankaranarayanan, 2018), and some of them have been found to have transporting activity on different metal ions.…”

Section: Introductionmentioning

confidence: 99%

The rice heavy‐metal transporter OsNRAMP1 regulates disease resistance by modulating ROS homoeostasis

Chu

Huang

Liu

et al. 2022

Plant Cell & Environment

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Crop diseases threaten food security and sustainable agriculture. Consumption of crops containing nonessential toxic metals leads to health risks for humans. Therefore, cultivation of disease-resistant and toxic metal-safe crops is a double-gain strategy that can contribute to food security. Here, we show that rice heavy-metal transporter OsNRAMP1 plays an important role in plant immunity by modulating metal ion and reactive oxygen species (ROS) homoeostasis. OsNRAMP1 expression was induced after pathogenic bacteria and fungi infections. The osnramp1 mutants had an increased content of H 2 O 2 and activity of superoxide dismutase, but decreased activity of catalase, showing enhanced broad-spectrum resistance against bacterial and fungal pathogens. RNA-seq analysis identified a number of differentially expressed genes that were involved in metal ion and ROS homoeostasis. Altered expression of metal ion-dependent ROS-scavenging enzymes genes and lower accumulation of cations such as Mn together induced compromised metal ion-dependent enzyme-catalysing activity and modulated ROS homoeostasis, which together contributed towards disease resistance in osnramp1 mutants. Furthermore, the osnramp1 mutants contained lower levels of toxic heavy metals Cd and Pb and micronutrients Ni and Mn in leaves and grains. Taken together, a proof of concept was achieved that broad-spectrum disease-resistant and toxic heavy-metal-safe rice was engineered by removal of the OsNRAMP1 gene.

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“…In yeast, three Nramps regulate the uptake of Mn 2+ , Cu 2+ , Co 2+ , and Cd 2+ (Supek et al 1996(Supek et al , 1997Liu et al 1997;Chen et al 1999). Moreover, the massive research revealed that the most important physiological substrate for Nramps is Mn 2+ (Bozzi and Gaudet 2021). Therefore, it is not surprising that AoNramp1 does not play an important role in Fe transport in A. oryzae.…”

Section: Discussionmentioning

confidence: 99%

Identification and characterization of Nramp transporter AoNramp1 in Aspergillus oryzae

Fan

Zhang

et al. 2021

3 Biotech

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The Nramp (natural resistance-associated macrophage protein) family of genes has been identified and characterized widely in many species. However, the Nramp genes and their characterizations have not been reported for Aspergillus oryzae. Here, only one Nramp gene AoNramp1 in A. oryzae genome was identified. Phylogenetic analysis revealed that AoNramp1 is not clustered with Nramps from yeast genus. Expression analysis showed that the transcript level of AoNramp1 was strongly induced under both Zn/Mn-replete and -deplete conditions. The GUS-staining assay indicated that the expression of AoN-ramp1 was strongly induced by Zn/Mn. Moreover, the AoNramp1 deletion and overexpression strains were constructed by the CRISPR/Cas9 system and A. oryzae amyB promoter, respectively. Phenotypic analysis showed that overexpression and deletion of AoNramp1 caused growth defects under Zn/Mn-deplete and -replete conditions, including mycelium growth and conidia formation. Together, these findings provide valuable information for further study on the biological roles of AoNramp1 in A. oryzae.

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Molecular Mechanism of Nramp-Family Transition Metal Transport

Cited by 59 publications

References 208 publications

A solid-supported membrane electrophysiology assay for efficient characterization of ion-coupled transport

A solid-supported membrane electrophysiology assay for efficient characterization of ion-coupled transport

The rice heavy‐metal transporter OsNRAMP1 regulates disease resistance by modulating ROS homoeostasis

Identification and characterization of Nramp transporter AoNramp1 in Aspergillus oryzae

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