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

Content Provider	PubMed Central
Author	Loiseau, Laurent Gerez, Catherine Bekker, Martijn Ollagnier-de, Choudens Sandrine Py, Béatrice Yannis, Sanakis Mattos, Joost Teixeira De Marc, Fontecave Barras, Frédéric
Copyright Year	2007
Abstract	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.
Related Links	http://dx.doi.org/10.1073/pnas.0705829104
Ending Page	13631
Page Count	6
Starting Page	13626
File Format	PDF
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	34
Volume Number	104
Language	English
Publisher	National Academy of Sciences
Publisher Date	2007-08-21
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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