Volume 4 - 2013 | <a class="ArticleLayoutHeader__info__doi" href="https://doi.org/10.3389/fpls.2013.00348">https://doi.org/10.3389/fpls.2013.00348</a>
This article is part of the Research TopicCellular Iron homeostasis and metabolism in plant<a class="Link Link--linkType Link--maincolor Link--medium Link--icon Link--chevronRight Link--right" aria-label="View all 16 articles" href="https://www.frontiersin.org/research-topics/1027/cellular-iron-homeostasis-and-metabolism-in-plant/magazine" target="_self" data-event="customLink-linkType-a_viewAll16Articles">View all 16 articles</a>
Iron (Fe) is an essential nutrient for plants and although the mechanisms controlling iron uptake from the soil are relatively well understood
comparatively little is known about subcellular trafficking of iron in plant cells
Mitochondria represent a significant iron sink within cells
as iron is required for the proper functioning of respiratory chain protein complexes
Mitochondria are a site of Fe&#x02013;S cluster synthesis
Here we review recent insights into the molecular mechanisms controlling mitochondrial iron transport and homeostasis
We focus on the recent identification of a mitochondrial iron uptake transporter in rice and a possible role for metalloreductases in iron uptake by mitochondria
we highlight recent advances in mitochondrial iron homeostasis with an emphasis on the roles of frataxin and ferritin in iron trafficking and storage within mitochondria
and wheat) tend to be poor sources of dietary iron and thus significant interest surrounds efforts to develop crop varieties with elevated levels of bioavailable iron
the Fe species that are available for transport into subcellular compartments are unclear at this time
we discuss in detail the roles of the iron transporter (MIT)
FH and ferritin in mitochondrial iron homeostasis
A working model of iron trafficking and utilization in plant mitochondria
Cytosolic Fe3+ (red circles) may be reduced to Fe2+ (blue circles) by a member of the ferric reductase oxidase (FRO) family within the inter-membrane space (IMS)
Ferrous iron is then translocated across the inner membrane by MIT
FH distributes this Fe to ISC assembly proteins and possibly to the heme biosynthetic machinery
Iron released from FER4 upon Fe deficiency may require the activity of another reductase prior to its utilization/remobilization
Mitochondrial iron exporters (MIEs) are postulated to function in mitochondrial iron export for delivery of iron to CIA
MCF proteins were first characterized in yeast and their crystal structure shows the presence of a tripartite structure with a total of six transmembrane helices
Amino acid residues responsible for substrate recognition are found in helices II
the gene encoding vacuolar iron transporter1 (VIT1) is upregulated
suggesting that excess cytosolic iron may be directed toward vacuoles
MIT plays an important role in seed development and its expression level is positively regulated by iron availability
consistent with the idea that it is essential for mitochondrial iron metabolism
Previous studies conducted in yeast and mammals have demonstrated an adverse effect of loss of mitochondrial iron transport on heme and Fe&#x02013;S cluster synthesis (<a href="#B65">Zhang et al., 2005</a>; <a href="#B46">Shaw et al., 2006</a>; <a href="#B66">Zhang et al., 2006</a>)
partial loss of MIT results in decreased total and mitochondrial aconitase activity
indicating that the effect on Fe&#x02013;S cluster synthesis affects not only mitochondrial Fe&#x02013;S proteins but also cytosolic Fe&#x02013;S cluster proteins
the role of MIT in heme synthesis has yet to be determined
the fact that mit loss-of-function lines show altered chlorophyll concentration and altered ferritin expression supports the idea of cross-talk between mitochondrial and chloroplastic iron homeostasis
2,5-DHBA is synthesized by a short chain dehydrogenase/reductase family member (BDH2)
BLAST searches of the Arabidopsis and rice genomes indicate that these genomes code for 3 and 13 BDH2 homologs respectively
Characterization of these homologs may give interesting insights into the mitochondrial iron trafficking pathways in plants
Rice possesses only two FRO family members, OsFRO1 and OsFRO2, neither of which has been shown to localize to mitochondria (<a href="#B54">Victoria Fde et al., 2012</a>; <a href="#B55">Vigani, 2012</a>)
iron uptake by mitochondria of grass species such as rice may differ from non-grass species
It is possible that iron uptake by rice mitochondria utilizes a non-reductive iron uptake pathway and/or the rice genome may encode other types of reductases capable of reducing iron
it will be critical to determine the redox state of iron transported across the outer and inner membranes of the mitochondria
This interaction thus links the accumulation of iron (bound to FH) with Fe&#x02013;S cluster production in a mitochondrion
the process is not described in plant systems
Recent studies have begun to shed light on the machinery involved in mitochondrial iron uptake, storage, and trafficking/utilization. In particular, studies of mitochondrial iron transporters, chaperones, and storage proteins have set the stage for future investigations in this area (see Figure <a href="#F1">1</a>)
Such studies will be critical to efforts to understand both organellar iron homeostasis and the mechanisms employed by plants to coordinate and prioritize Fe utilization by the various iron containing compartments of the cell
These studies will contribute to the development of a comprehensive understanding of iron homeostasis in plants
which should enable efforts to develop crop varieties with improved tolerance of growth on iron-limited soils and elevated levels of bioavailable iron in support of improved sustainability in agriculture and reductions in the incidence of iron deficiency in humans
The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest
The authors are grateful to Grandon Wilson for critical reading of the manuscript and gratefully acknowledge support from the US NSF (IOS 0919739)
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two suppressors of mtRNA splicing defects in yeast
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Frataxin-mediated iron delivery to ferrochelatase in the final step of heme biosynthesis
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Evidence for the presence of ferritin in plant mitochondria
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Frataxin and mitochondrial carrier proteins
cooperate in providing iron for heme synthesis
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and frataxin provide iron for Fe&#x02013;S cluster synthesis in mitochondria
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Iron and hydrogen peroxide detoxification properties of DNA-binding protein from starved cells
A ferritin-like DNA-binding protein of Escherichia coli
<a href="http://www.ncbi.nlm.nih.gov/sites/entrez?Db=pubmed&#x00026;Cmd=ShowDetailView&#x00026;TermToSearch=12016214" target="_blank">Pubmed Abstract</a> | <a href="http://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?db=pubmed&#x00026;cmd=prlinks&#x00026;retmode=ref&#x00026;id=12016214" target="_blank">Pubmed Full Text</a> | <a href="http://dx.doi.org/10.1074/jbc.M202094200" target="_blank">CrossRef Full Text</a>
Citation: Jain A and Connolly EL (2013) Mitochondrial iron transport and homeostasis in plants. Front. Plant Sci. 4:348. <a href="http://dx.doi.org/10.3389/fpls.2013.00348">doi: 10.3389/fpls.2013.00348</a>
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*Correspondence: Erin L. Connolly, University of South Carolina, 715 Sumter Street, Columbia, SC 29208, USA e-mail:<a id="encmail">ZXJpbmNAYmlvbC5zYy5lZHU=</a>
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