Isoprenoid biosynthesis in chloroplasts via the methylerythritol phosphate pathway: the (E)-4-hydroxy-3-methylbut-2-enyl diphosphate synthase (GcpE) from Arabidopsis thaliana is a [4Fe?4S] protein

Seemann, Myriam; Wegner, Patrick A.; Schünemann, Volker; Bui, Bernadette Tse Sum; Wolff, Murielle; Marquet, Andrée; Trautwein, Alfred X.; Rohmer, Michel

doi:10.1007/s00775-004-0619-z

Cited by 75 publications

(92 citation statements)

References 38 publications

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“…4A) and show diamagnetic ground states of both species. This spectroscopic signature is again indicative for [4Fe-4S] 2ϩ clusters (25,33). Species 3 with ␦ 3 ϭ 0.26 mm/s, ⌬E Q3 ϭ 0.63 mm/s, and a relative contribution of 12% (Fig.…”

Section: Expression and Isolation Of Abce1-mentioning

confidence: 67%

“…4B). The isomer shifts of species 1 and 2 are characteristic for Fe 2.5ϩ pairs of [4Fe-4S] 2ϩ clusters (25,33). Fig.…”

Section: Expression and Isolation Of Abce1-mentioning

confidence: 99%

“…4A) does lead to a broad magnetic background in the high field spectrum. Such behavior is characteristic for an unspecific Fe 3ϩ (33). Therefore, species 3 has been disregarded in the simulation.…”

Section: Expression and Isolation Of Abce1-mentioning

confidence: 99%

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Structural Organization of Essential Iron-Sulfur Clusters in the Evolutionarily Highly Conserved ATP-binding Cassette Protein ABCE1

Barthelme

Scheele

Dinkelaker

et al. 2007

Journal of Biological Chemistry

107

110

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The ABC protein ABCE1, formerly named RNase L inhibitor RLI1, is one of the most conserved proteins in evolution and is expressed in all organisms except eubacteria. Because of its fundamental role in translation initiation and/or ribosome biosynthesis, ABCE1 is essential for life. Its molecular mechanism has, however, not been elucidated. In addition to two ABC ATPase domains, ABCE1 contains a unique N-terminal region with eight conserved cysteines, predicted to coordinate iron-sulfur clusters. Here we present detailed information on the type and on the structural organization of the Fe-S clusters in ABCE1.

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Section: Expression and Isolation Of Abce1-mentioning

confidence: 67%

“…4B). The isomer shifts of species 1 and 2 are characteristic for Fe 2.5ϩ pairs of [4Fe-4S] 2ϩ clusters (25,33). Fig.…”

Section: Expression and Isolation Of Abce1-mentioning

confidence: 99%

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Structural Organization of Essential Iron-Sulfur Clusters in the Evolutionarily Highly Conserved ATP-binding Cassette Protein ABCE1

Barthelme

Scheele

Dinkelaker

et al. 2007

Journal of Biological Chemistry

107

110

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“…5B) showed a slightly asymmetric doublet (97% relative area), which is consistent with a [4Fe-4S] 2ϩ (S ϭ 0) cluster. This species was simulated with two doublets, I and II, at a 3:1 ratio as indicated by Seeman et al (41). The analysis gave the following parameters for these doublets: I, ␦ ϭ 0.47 mm/s and ⌬E Q ϭ 1.00 mm/s and for doublet II, ␦ ϭ 0.48 mm/s and ⌬E Q ϭ 1.34 mm/s.…”

Section: The Eukaryotic Mevalonate (Mva)-dependent Pathway Allowedmentioning

confidence: 99%

ErpA, an iron–sulfur (Fe–S) protein of the A-type essential for respiratory metabolism in Escherichia coli

Loiseau

Gerez

Bekker

et al. 2007

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

134

149

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Understanding the biogenesis of iron-sulfur (Fe-S) proteins is relevant to many fields, including bioenergetics, gene regulation, and cancer research. Several multiprotein complexes assisting Fe-S assembly have been identified in both prokaryotes and eukaryotes. Here, we identify in Escherichia coli an A-type Fe-S protein that we named ErpA. Remarkably, erpA was found essential for growth of E. coli in the presence of oxygen or alternative electron acceptors. It was concluded that isoprenoid biosynthesis was impaired by the erpA mutation. First, the eukaryotic mevalonate-dependent pathway for biosynthesis of isopentenyl diphosphate restored the respiratory defects of an erpA mutant. Second, the erpA mutant contained a greatly reduced amount of ubiquinone and menaquinone. Third, ErpA bound Fe-S clusters and transferred them to apo-IspG, a protein catalyzing isopentenyl diphosphate biosynthesis in E. coli. Surprisingly, the erpA gene maps at a distance from any other Fe-S biogenesis-related gene. ErpA is an A-type Fe-S protein that is characterized by an essential role in cellular metabolism.essential gene yadR ͉ isoprenoid ͉ respiration ͉ scaffold

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“…Recent data has shown that (E)-4-hydroxy-3-methylbut-2-enyl diphosphate synthase (GcpE) and LytB proteins are iron-sulfur proteins containing a [4Fe-4S] 2ϩ cluster after reconstitution of the purified protein (12)(13)(14). GcpE catalyzes the reduction of MEcPP into HMBPP via two successive one-electron transfers (11,13).…”

mentioning

confidence: 99%

Cyanobacterial Non-mevalonate Pathway

Okada

Hase

2005

Journal of Biological Chemistry

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(E)-4-Hydroxy-3-methylbut-2-enyl diphosphate synthase (GcpE), which catalyzes the conversion of 2-Cmethyl-D-erythritol cyclodiphosphate (MEcPP) into (E)-4-hydroxy-3-methylbut-2-enyl diphosphate (HMBPP), is an essential enzyme of the non-mevalonate (2-C-methyl-D-erythritol-4-phosphate (MEP)) pathway for isoprenoid biosynthesis. The terminal steps of the MEP pathway are still not fully understood, although this pathway is necessary for survival in various organisms such as cyanobacteria, plastids of algae and higher plants, and the apicoplast of human malaria parasites. To determine the efficient redox partner for thermophilic cyanobacterial GcpE, We have expressed the gcpE and petF genes in Escherichia coli and studied the protein-protein interaction of GcpE protein with ferredoxin I (PetF) from the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1. Recombinant GcpE protein was purified by an N-terminal His 6 tag and reconstituted as a [4Fe-4S] 2؉ metalloprotein. GcpE was shown to interact strongly with PetF via the bacterial two-hybrid system designed to detect protein-protein interactions. Moreover, a direct protein-protein interaction between PetF and GcpE was confirmed in an in vitro glutathione Stransferase (GST) pull-down assay. To investigate electron transfer activity from PetF to GcpE, we also constructed a NADPH-dependent reducing shuttle system with purified recombinant ferredoxin-NADP ؉ oxidoreductase (PetH) and PetF. The result demonstrated that PetF has the ability to transfer electrons to GcpE. Thus, the combined data provide the first evidence that GcpE is a ferredoxin-dependent enzyme in T. elongatus BP-1.

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Isoprenoid biosynthesis in chloroplasts via the methylerythritol phosphate pathway: the (E)-4-hydroxy-3-methylbut-2-enyl diphosphate synthase (GcpE) from Arabidopsis thaliana is a [4Fe?4S] protein

Cited by 75 publications

References 38 publications

Structural Organization of Essential Iron-Sulfur Clusters in the Evolutionarily Highly Conserved ATP-binding Cassette Protein ABCE1

Structural Organization of Essential Iron-Sulfur Clusters in the Evolutionarily Highly Conserved ATP-binding Cassette Protein ABCE1

ErpA, an iron–sulfur (Fe–S) protein of the A-type essential for respiratory metabolism in Escherichia coli

Cyanobacterial Non-mevalonate Pathway

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