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Raven, John A.; Evans, M.C.W.; Korb, Rebecca E.

doi:10.1023/a:1006282714942

Cited by 546 publications

(161 citation statements)

References 255 publications

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“…Fe-S cluster formation and repair are therefore important areas of study, because Fe-S proteins are involved in vital processes in organisms ranging from bacteria to mammals (1,2,43). Similarly, in plants, Fe-S proteins have been identified as playing important roles (29)(30)(31)33). Despite this, little is known about Fe-S cluster biogenesis in plants and in particular the repair of damaged clusters.…”

Section: Discussionmentioning

confidence: 99%

“…The identification of both mitochondrial and plastidic NFU Fe-S cluster biogenesis proteins in Arabidopsis (28) has further underlined this fact. In chloroplasts Fe-S clusters are required for a functional cytochrome b 6 ͞f complex, ferredoxin, and photosystem I, ensuring electron flow in the thylakoids (29,30). Interestingly, the chloroplast import protein Tic55 contains an Fe-S cluster and may be involved in redox regulation during chloroplast protein import (31).…”

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confidence: 99%

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AtNAP7 is a plastidic SufC-like ATP-binding cassette/ATPase essential for Arabidopsis embryogenesis

Møller

2004

Proc. Natl. Acad. Sci. U.S.A.

124

107

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In bacteria, yeast, and mammals, iron-sulfur (Fe-S) cluster-containing proteins are involved in numerous processes including electron transfer, metabolic reactions, sensing, signaling, and regulation of gene expression. In humans, iron-storage diseases such as X-linked sideroblastic anemia and ataxia are caused by defects in Fe-S cluster availability. The biogenesis of Fe-S clusters involves several pathways, and in bacteria, the SufABCDSE operon has been shown to play a vital role in Fe-S biogenesis and repair during oxidative stress. Although Fe-S proteins play vital roles in plants, Fe-S cluster biogenesis and maintenance and physiological consequences of dysfunctional Fe-S cluster assembly remains obscure. Here we report that Arabidopsis plants deficient for the SufC homolog AtNAP7 show lethality at the globular stage of embryogenesis. AtNAP7 is expressed in developing embryos and in apical, root, and floral meristems and encodes an ATP-binding cassette͞ATPase that can partially rescue growth defects in an Escherichia coli SufC mutant during oxidative stress. AtNAP7 is plastid-localized, and mutant embryos contain abnormal developing plastids with disorganized thylakoid structures. We found that AtNAP7 can interact with AtNAP6, a plastidic Arabidopsis SufD homolog, and because Arabidopsis plastids also harbor SufA, SufB, SufS, and SufE homologs, plastids probably contain a complete SUF system. Our results imply that AtNAP7 represents a conserved SufC protein involved in the biogenesis and͞or repair of oxidatively damaged Fe-S clusters and suggest an important role for plastidic Fe-S cluster maintenance and repair during Arabidopsis embryogenesis.

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

AtNAP7 is a plastidic SufC-like ATP-binding cassette/ATPase essential for Arabidopsis embryogenesis

Møller

2004

Proc. Natl. Acad. Sci. U.S.A.

124

107

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“…5B). CpNifS silencing did not affect the D1 protein, a component of the PSII reaction center in which no Fe-S clusters are present (18), suggesting that most PSII was intact. In contrast, components of the cytochrome b 6 LhcI).…”

Section: Levels Of Chloroplastic Fe-s Proteins Are Reduced By Cpnifs mentioning

confidence: 92%

Chloroplast iron-sulfur cluster protein maturation requires the essential cysteine desulfurase CpNifS

Hoewyk

Abdel‐Ghany

Cohu

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

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NifS-like proteins provide the sulfur (S) for the formation of iron-sulfur (Fe-S) clusters, an ancient and essential type of cofactor found in all three domains of life. Plants are known to contain two distinct NifS-like proteins, localized in the mitochondria (MtNifS) and the chloroplast (CpNifS). In the chloroplast, five different Fe-S cluster types are required in various proteins. These plastid Fe-S proteins are involved in a variety of biochemical pathways including photosynthetic electron transport and nitrogen and sulfur assimilation. In vitro, the chloroplastic cysteine desulfurase CpNifS can release elemental sulfur from cysteine for Fe-S cluster biogenesis in ferredoxin. However, because of the lack of a suitable mutant allele, the role of CpNifS has not been studied thus far in planta. To study the role of CpNifS in Fe-S cluster biogenesis in vivo, the gene was silenced by using an inducible RNAi (interference) approach. Plants with reduced CpNifS expression exhibited chlorosis, a disorganized chloroplast structure, and stunted growth and eventually became necrotic and died before seed set. Photosynthetic electron transport and carbon dioxide assimilation were severely impaired in the silenced plant lines. The silencing of CpNifS decreased the abundance of all chloroplastic Fe-S proteins tested, representing all five Fe-S cluster types. Mitochondrial Fe-S proteins and respiration were not affected, suggesting that mitochondrial and chloroplastic Fe-S assembly operate independently. These findings indicate that CpNifS is necessary for the maturation of all plastidic Fe-S proteins and, thus, essential for plant growth.Fe-S proteins ͉ inducible RNAi ͉ photosynthesis ͉ Arabidopsis thaliana

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“…Further details and references are given in the text and in [10][11][12]101,105,106,110,[112][113][114][115][116][117][118][119][120]. Predicted resource costs of synthesizing and operating a photosynthetic apparatus using a CCM relative to one relying on entry of CO 2 by diffusion [66,[68][69][70][71]73,91,105,121] Pleistocene, they would have had to have survived intervening period(s) of higher CO 2 and higher temperatures. The mechanisms of retention of CCMs in these apparently unfavourable environments are now considered in the context of the response of present day CCMs to such environments.…”

Section: The Origins Of Co 2 -Concentrating Mechanismsmentioning

confidence: 99%

Algal evolution in relation to atmospheric CO ₂ : carboxylases, carbon-concentrating mechanisms and carbon oxidation cycles

Raven

Giordano

Beardall

et al. 2012

Phil. Trans. R. Soc. B

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247

209

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Oxygenic photosynthesis evolved at least 2.4 Ga; all oxygenic organisms use the ribulose bisphosphate carboxylase-oxygenase (Rubisco) -photosynthetic carbon reduction cycle (PCRC) rather than one of the five other known pathways of autotrophic CO 2 assimilation. The high CO 2 and (initially) O 2 -free conditions permitted the use of a Rubisco with a high maximum specific reaction rate. As CO 2 decreased and O 2 increased, Rubisco oxygenase activity increased and 2-phosphoglycolate was produced, with the evolution of pathways recycling this inhibitory product to sugar phosphates. Changed atmospheric composition also selected for Rubiscos with higher CO 2 affinity and CO 2 /O 2 selectivity correlated with decreased CO 2 -saturated catalytic capacity and/or for CO 2 -concentrating mechanisms (CCMs). These changes increase the energy, nitrogen, phosphorus, iron, zinc and manganese cost of producing and operating Rubisco -PCRC, while biosphere oxygenation decreased the availability of nitrogen, phosphorus and iron. The majority of algae today have CCMs; the timing of their origins is unclear. If CCMs evolved in a low-CO 2 episode followed by one or more lengthy high-CO 2 episodes, CCM retention could involve a combination of environmental factors known to favour CCM retention in extant organisms that also occur in a warmer high-CO 2 ocean. More investigations, including studies of genetic adaptation, are needed.

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Cited by 546 publications

References 255 publications

AtNAP7 is a plastidic SufC-like ATP-binding cassette/ATPase essential for Arabidopsis embryogenesis

AtNAP7 is a plastidic SufC-like ATP-binding cassette/ATPase essential for Arabidopsis embryogenesis

Chloroplast iron-sulfur cluster protein maturation requires the essential cysteine desulfurase CpNifS

Algal evolution in relation to atmospheric CO ₂ : carboxylases, carbon-concentrating mechanisms and carbon oxidation cycles

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Untitled

Cited by 546 publications

References 255 publications

AtNAP7 is a plastidic SufC-like ATP-binding cassette/ATPase essential for Arabidopsis embryogenesis

AtNAP7 is a plastidic SufC-like ATP-binding cassette/ATPase essential for Arabidopsis embryogenesis

Chloroplast iron-sulfur cluster protein maturation requires the essential cysteine desulfurase CpNifS

Algal evolution in relation to atmospheric CO 2 : carboxylases, carbon-concentrating mechanisms and carbon oxidation cycles

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Algal evolution in relation to atmospheric CO ₂ : carboxylases, carbon-concentrating mechanisms and carbon oxidation cycles