Isoprenoid biosynthesis via the methylerythritol phosphate pathway: the (<i>E</i>)‐4‐hydroxy‐3‐methylbut‐2‐enyl diphosphate reductase (LytB/IspH) from <i>Escherichia coli</i> is a [4Fe–4S] protein

Wolff, Murielle; Seemann, Myriam; Bui, Bernadette Tse Sum; Frapart, Yves-Michel; Tritsch, Denis; Estrabot, Ana Garcia; Rodríguez‐Concepción, Manuel; Boronat, Albert; Marquet, Andrée; Rohmer, Michel

doi:10.1016/s0014-5793(03)00317-x

Cited by 166 publications

(250 citation statements)

References 35 publications

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“…8). The E. coli IspH protein is a reductase that possesses a dioxygen-sensitive [4Fe-4S] cluster (Wolff et al, 2003). Amino acid sequence alignment reveals that the Cys residues that may be involved in iron-sulfur cluster formation and the His residues that may be involved in proton-transfer reactions are also conserved in the Arabidopsis IspH protein (Botella-Pavia et al, 2004).…”

Section: Discussionmentioning

confidence: 99%

The Arabidopsis IspH Homolog Is Involved in the Plastid Nonmevalonate Pathway of Isoprenoid Biosynthesis

2005

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Plant isoprenoids are synthesized via two independent pathways, the cytosolic mevalonate (MVA) pathway and the plastid nonmevalonate pathway. The Escherichia coli IspH (LytB) protein is involved in the last step of the nonmevalonate pathway. We have isolated an Arabidopsis (Arabidopsis thaliana) ispH null mutant that has an albino phenotype and have generated Arabidopsis transgenic lines showing various albino patterns caused by IspH transgene-induced gene silencing. The initiation of albino phenotypes rendered by IspH gene silencing can arise independently from multiple sites of the same plant. After a spontaneous initiation, the albino phenotype is systemically spread toward younger tissues along the source-to-sink flow relative to the initiation site. The development of chloroplasts is severely impaired in the IspH-deficient albino tissues. Instead of thylakoids, mutant chloroplasts are filled with vesicles. Immunoblot analysis reveals that Arabidopsis IspH is a chloroplast stromal protein. Expression of Arabidopsis IspH complements the lethal phenotype of an E. coli ispH mutant. In 2-week-old Arabidopsis seedlings, the expression of 1-deoxy-d-xylulose 5-phosphate synthase (DXS), 1-deoxy-d-xylulose 5-phosphate reductoisomerase (DXR), IspD, IspE, IspF, and IspG genes is induced by light, whereas the expression of the IspH gene is constitutive. The addition of 3% sucrose in the media slightly increased levels of DXS, DXR, IspD, IspE, and IspF mRNA in the dark. In a 16-h-light/8-h-dark photoperiod, the accumulation of the IspH transcript oscillates with the highest levels detected in the early light period (2–6 h) and the late dark period (4–6 h). The expression patterns of DXS and IspG are similar to that of IspH, indicating that these genes are coordinately regulated in Arabidopsis when grown in a 16-h-light/8-h-dark photoperiod

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Section: Discussionmentioning

confidence: 99%

The Arabidopsis IspH Homolog Is Involved in the Plastid Nonmevalonate Pathway of Isoprenoid Biosynthesis

2005

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“…The E. coli HDR is an iron-sulfur protein that is sensitive to oxygen. 30 The critical Cys residues involved in iron-sulfur cluster formation are conserved in plant and cyanobacterial HDRs. 21 It is likely that the HDR enzyme is also an iron-sulfur protein in these oxygen-evolving www.tandfonline.com e988072-3 Plant Signaling & Behavior photosynthetic organisms.…”

Section: -29mentioning

confidence: 99%

The amino-terminal conserved domain of 4-hydroxy-3-methylbut-2-enyl diphosphate reductase is critical for its function in oxygen-evolving photosynthetic organisms

Hsieh

2015

Plant Signaling & Behavior

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“…We made the assumption that the respiration defect was related to alteration of quinone pools. Indeed, quinone derivatives are electron carriers used by both anaerobic and aerobic respiratory chains and are derived from IPP, whose synthesis in bacteria depends on two essential [4Fe-4S] cluster-containing proteins, namely IspG (formally GcpE) and IspH (formally LytB) (38,39). The erpA null mutation (⌬erpA::cat) was introduced into an engineered E. coli strain, which can synthesize IPP both by its natural endogenous pathway and by the eukaryotic MVA-dependent pathway, a pathway that does not employ Fe-S enzymes (40).…”

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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Isoprenoid biosynthesis via the methylerythritol phosphate pathway: the (E)‐4‐hydroxy‐3‐methylbut‐2‐enyl diphosphate reductase (LytB/IspH) from Escherichia coli is a [4Fe–4S] protein

Cited by 166 publications

References 35 publications

The Arabidopsis IspH Homolog Is Involved in the Plastid Nonmevalonate Pathway of Isoprenoid Biosynthesis

The Arabidopsis IspH Homolog Is Involved in the Plastid Nonmevalonate Pathway of Isoprenoid Biosynthesis

The amino-terminal conserved domain of 4-hydroxy-3-methylbut-2-enyl diphosphate reductase is critical for its function in oxygen-evolving photosynthetic organisms

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

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