Stimulation of the ATPase activity of the yeast mitochondrial ABC transporter Atm1p by thiol compounds

Kuhnke, Grit; Neumann, K.; Mühlenhoff, Ulrich; Lill, Roland

doi:10.1080/09687860500473630

Cited by 68 publications

(83 citation statements)

References 49 publications

(53 reference statements)

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“…However, other possibilities cannot be ruled out, for example that ATM3 transports multiple substrates, including the pterin precursor of Moco. In support of a sulfide derivative as substrate, it was shown that the ATPase activity of yeast Atm1p is stimulated by thiol compounds in vitro (Kuhnke et al, 2006). Although it has been suggested that ATM3 transports cadmium, our finding that cadmium has little effect on root length in atm3 mutants (Fig.…”

Section: Discussioncontrasting

confidence: 52%

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An Allelic Mutant Series of ATM3 Reveals Its Key Role in the Biogenesis of Cytosolic Iron-Sulfur Proteins in Arabidopsis

et al. 2009

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The ATP-binding cassette transporters of mitochondria (ATMs) are highly conserved proteins, but their function in plants is poorly defined. Arabidopsis (Arabidopsis thaliana) has three ATM genes, namely ATM1, ATM2, and ATM3. Using a collection of insertional mutants, we show that only ATM3 has an important function for plant growth. Additional atm3 alleles were identified among sirtinol-resistant lines, correlating with decreased activities of aldehyde oxidases, cytosolic enzymes that convert sirtinol into an auxin analog, and depend on iron-sulfur (Fe-S) and molybdenum cofactor (Moco) as prosthetic groups. In the sirtinol-resistant atm3-3 allele, the highly conserved arginine-612 is replaced by a lysine residue, the negative effect of which could be mimicked in the yeast Atm1p ortholog. Arabidopsis atm3 mutants displayed defects in root growth, chlorophyll content, and seedling establishment. Analyses of selected metal enzymes showed that the activity of cytosolic aconitase (Fe-S) was strongly decreased across the range of atm3 alleles, whereas mitochondrial and plastid Fe-S enzymes were unaffected. Nitrate reductase activity (Moco, heme) was decreased by 50% in the strong atm3 alleles, but catalase activity (heme) was similar to that of the wild type. Strikingly, in contrast to mutants in the yeast and mammalian orthologs, Arabidopsis atm3 mutants did not display a dramatic iron homeostasis defect and did not accumulate iron in mitochondria. Our data suggest that Arabidopsis ATM3 may transport (1) at least two distinct compounds or (2) a single compound required for both Fe-S and Moco assembly machineries in the cytosol, but not iron.

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Section: Discussioncontrasting

confidence: 52%

“…Although ATM3, and therefore the substrate, is required for cytosolic Fe-S clusters, it is unlikely to be an Fe-S cluster. First, free Fe-S is unstable and would need to be liganded, for instance by a small peptide (Kuhnke et al, 2006). Second, iron does not accumulate in the mitochondria of atm3 mutants (Fig.…”

Section: Discussionmentioning

confidence: 99%

An Allelic Mutant Series of ATM3 Reveals Its Key Role in the Biogenesis of Cytosolic Iron-Sulfur Proteins in Arabidopsis

et al. 2009

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“…ABC transporters use the binding and hydrolysis of ATP to power the movement of substrates. Surprisingly, many ABC transporters exhibit a basal ATPase activity in vitro in the absence of transport substrate, which is stimulated between 2-and 10-fold when a transport substrate is added (25)(26)(27). ABCB10 showed basal ATPase activity, with apparent kinetic parameters similar to those of other ABC transporters (28,29), when it was purified in DDM and either CHS or CDL, with or without reconstitution into liposomes (Table 1, Fig.…”

Section: Structure Abcb10 In Complex With Nucleotide Analogs and Withoutmentioning

confidence: 99%

Structures of ABCB10, a human ATP-binding cassette transporter in apo- and nucleotide-bound states

Shintre

Pike

et al. 2013

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

220

181

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ABCB10 is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria. In mammals ABCB10 is essential for erythropoiesis, and for protection of mitochondria against oxidative stress. ABCB10 is therefore a potential therapeutic target for diseases in which increased mitochondrial reactive oxygen species production and oxidative stress play a major role. The crystal structure of apo-ABCB10 shows a classic exporter fold ABC transporter structure, in an open-inwards conformation, ready to bind the substrate or nucleotide from the inner mitochondrial matrix or membrane. Unexpectedly, however, ABCB10 adopts an openinwards conformation when complexed with nonhydrolysable ATP analogs, in contrast to other transporter structures which adopt an open-outwards conformation in complex with ATP. The three complexes of ABCB10/ATP analogs reported here showed varying degrees of opening of the transport substrate binding site, indicating that in this conformation there is some flexibility between the two halves of the protein. These structures suggest that the observed plasticity, together with a portal between two helices in the transmembrane region of ABCB10, assist transport substrate entry into the substrate binding cavity. These structures indicate that ABC transporters may exist in an open-inwards conformation when nucleotide is bound. We discuss ways in which this observation can be aligned with the current views on mechanisms of ABC transporters.ABC mitochondrial erythroid | X-ray crystallography | human membrane protein structure | nucleotide complex | cardiolipin

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“…If the mitochondrial pool of NFS1 provides a sulfur-containing precursor for the CIA pathway, then this needs to be exported to the cytosol via a transporter. A probable candidate is the ABC transporter of the mitochondria, Atm1 in yeast [14,15]. The orthologues in mammals (ABCB7) and plants (ATM3) are also required for the activity of cytosolic Fe-S enzymes [16][17][18].…”

Section: Introductionmentioning

confidence: 99%

Requirements of the cytosolic iron–sulfur cluster assembly pathway in Arabidopsis

Bernard

Netz

Lagny

et al. 2013

Phil. Trans. R. Soc. B

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The assembly of iron–sulfur (Fe–S) clusters requires dedicated protein factors inside the living cell. Striking similarities between prokaryotic and eukaryotic assembly proteins suggest that plant cells inherited two different pathways through endosymbiosis: the ISC pathway in mitochondria and the SUF pathway in plastids. Fe–S proteins are also found in the cytosol and nucleus, but little is known about how they are assembled in plant cells. Here, we show that neither plastid assembly proteins nor the cytosolic cysteine desulfurase ABA3 are required for the activity of cytosolic aconitase, which depends on a [4Fe–4S] cluster. In contrast, cytosolic aconitase activity depended on the mitochondrial cysteine desulfurase NFS1 and the mitochondrial transporter ATM3. In addition, we were able to complement a yeast mutant in the cytosolic Fe–S cluster assembly pathway, dre2 , with the Arabidopsis homologue AtDRE2 , but only when expressed together with the diflavin reductase AtTAH18 . Spectroscopic characterization showed that purified AtDRE2 could bind up to two Fe–S clusters. Purified AtTAH18 bound one flavin per molecule and was able to accept electrons from NAD(P)H. These results suggest that the proteins involved in cytosolic Fe–S cluster assembly are highly conserved, and that dependence on the mitochondria arose before the second endosymbiosis event leading to plastids.

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Stimulation of the ATPase activity of the yeast mitochondrial ABC transporter Atm1p by thiol compounds

Cited by 68 publications

References 49 publications

An Allelic Mutant Series of ATM3 Reveals Its Key Role in the Biogenesis of Cytosolic Iron-Sulfur Proteins in Arabidopsis

An Allelic Mutant Series of ATM3 Reveals Its Key Role in the Biogenesis of Cytosolic Iron-Sulfur Proteins in Arabidopsis

Structures of ABCB10, a human ATP-binding cassette transporter in apo- and nucleotide-bound states

Requirements of the cytosolic iron–sulfur cluster assembly pathway in Arabidopsis

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