SufC hydrolyzes ATP and interacts with SufB from <i>Thermotoga maritima</i>

Rangachari, K.; Davis, Colin T.; Eccleston, John F.; Hirst, Elizabeth; Saldanha, José W.; Strath, Malcolm; Wilson, Robert

doi:10.1016/s0014-5793(02)02369-4

Cited by 64 publications

(71 citation statements)

References 21 publications

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“…In fact, the individual SufB, SufC, and SufD proteins could only be completely separated from the complex using reverse phase high performance liquid chromatography, indicating tight association. This result is consistent with previous yeast two-hybrid (27) and fluorescence anisotropy (26) studies that suggest interactions between SufC and the SufB and SufD proteins. The SufBCD complex was in a folded conformation based on its CD spectra and also possessed ATPase activity (data not shown).…”

Section: Purification Of the Suf Proteins-thesupporting

confidence: 93%

“…SufA is a homologue of IscA and can form Fe-S clusters in vitro (25). SufC has the sequence hallmarks of the ATPase subunit of ABC transporters and has been shown to exhibit ATPase activity (26). The biochemical functions of SufB, SufD, and SufE are unknown, although fluorescence anisotropy and yeast two-hybrid assays indicate that SufB and SufD interact with SufC (26,27).…”

mentioning

confidence: 99%

“…SufC has the sequence hallmarks of the ATPase subunit of ABC transporters and has been shown to exhibit ATPase activity (26). The biochemical functions of SufB, SufD, and SufE are unknown, although fluorescence anisotropy and yeast two-hybrid assays indicate that SufB and SufD interact with SufC (26,27). Most of the suf genes are well conserved in a variety of microorganisms, including cyanobacteria, as well as in higher plants (28,29).…”

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confidence: 99%

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The SufE Protein and the SufBCD Complex Enhance SufS Cysteine Desulfurase Activity as Part of a Sulfur Transfer Pathway for Fe-S Cluster Assembly in Escherichia coli

Outten

Wood

Muñoz

et al. 2003

Journal of Biological Chemistry

267

375

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The sufABCDSE operon of the Gram-negative bacterium Escherichia coli is induced by oxidative stress and iron deprivation. To examine the biochemical roles of the Suf proteins, we purified all of the proteins and assayed their effect on SufS cysteine desulfurase activity. Here we report that the SufE protein can stimulate the cysteine desulfurase activity of the SufS enzyme up to 8-fold and accepts sulfane sulfur from SufS. This sulfur transfer process from SufS to SufE is sheltered from the environment based on its resistance to added reductants and on the analysis of available crystal structures of the proteins. We also found that the SufB, SufC, and SufD proteins associate in a stable complex and that, in the presence of SufE, the SufBCD complex further stimulates SufS activity up to 32-fold. Thus, the SufE protein and the SufBCD complex act synergistically to modulate the cysteine desulfurase activity of SufS. We propose that this sulfur transfer mechanism may be important for limiting sulfide release during oxidative stress conditions in vivo.

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Section: Purification Of the Suf Proteins-thesupporting

confidence: 93%

mentioning

confidence: 99%

mentioning

confidence: 99%

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The SufE Protein and the SufBCD Complex Enhance SufS Cysteine Desulfurase Activity as Part of a Sulfur Transfer Pathway for Fe-S Cluster Assembly in Escherichia coli

Outten

Wood

Muñoz

et al. 2003

Journal of Biological Chemistry

267

375

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“…The suf operon (sufABCDSE) represents the third Fe-S system, and recent studies have shown that Suf proteins are involved in Fe-S cluster biosynthesis and repair. SufB, SufC, and SufD are conserved in nature, and in bacteria SufC interacts with SufB and SufD in the cytosol (17,18). SufE interacts with SufS, involved in cysteine desulfuration (6), and SufA assembles Fe-S clusters transiently in vitro (19).…”

mentioning

confidence: 99%

“…Bacterial SufC can hydrolyze ATP and probably acts as an energizer for the Suf system (6,17,18). SufC represents an ATP-binding cassette (ABC) protein with no membranespanning domains (18), implying that it is soluble, although conflicting evidence suggests that SufC may be membranelocalized in E. coli (17).…”

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.

125

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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Iron–Sulfur Cluster Biogenesis in Archaea and Bacteria

Chahal

Boyd

Outten

2004

Encyclopedia of Inorganic and Bioinorganic Chemistry

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Iron–sulfur (Fe–S) clusters are key cofactors required for the activity of essential metalloproteins. Biogenesis of Fe–S clusters is carried out by multiple proteins that work together to mobilize iron and sulfide, assemble nascent clusters, and traffic them to target metalloproteins. While the Isc, Nif, and Suf pathways are the most well‐studied Fe–S cluster biogenesis systems, it is clear that a variety of accessory proteins and metabolites cooperate with these systems for cluster assembly. Here, we review the current status of Fe–S cluster biogenesis research in Bacteria and Archaea.

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SufC hydrolyzes ATP and interacts with SufB from Thermotoga maritima

Cited by 64 publications

References 21 publications

The SufE Protein and the SufBCD Complex Enhance SufS Cysteine Desulfurase Activity as Part of a Sulfur Transfer Pathway for Fe-S Cluster Assembly in Escherichia coli

The SufE Protein and the SufBCD Complex Enhance SufS Cysteine Desulfurase Activity as Part of a Sulfur Transfer Pathway for Fe-S Cluster Assembly in Escherichia coli

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

Iron–Sulfur Cluster Biogenesis in Archaea and Bacteria

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