Journal Article

PHPPUBDB-4359

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Structural organization of essential iron-sulfur clusters in the evolutionarily highly conserved ATP-binding cassette protein ABCE1

Barthelme, D. ; Scheele, U. ; Dinkeleker, S. ; Janoschka, A. ; MacMillan, F. ; Verena Albers, S. ; Driessen, A. J. M. ; Salomone Stagni, M. ; Bill, E. ; Meyer-Klaucke, W. ; Schunemann, V. ; Tampe, R. ; DESY

2007
Soc. Bethesda, Md.

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Please use a persistent id in citations: doi:10.1074/jbc.M700825200

Abstract: 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. Based on biophysical, biochemical, and yeast genetic analyses, ABCE1 harbors two essential diamagnetic [4Fe-4S](2+) clusters with different electronic environments, one ferredoxin-like (CPX(n)CX(2)CX(2)C; Cys at positions 4-7) and one unique ABCE1-type cluster (CXPX(2)CX(3)CX(n)CP; Cys at positions 1, 2, 3, and 8). Strikingly, only seven of the eight conserved cysteines coordinating the Fe-S clusters are essential for cell viability. Mutagenesis of the cysteine at position 6 yielded a functional ABCE1 with the ferredoxin-like Fe-S cluster in a paramagnetic [3Fe-4S](+) state. Notably, a lethal mutation of the cysteine at position 4 can be rescued by ligand swapping with an adjacent, extra cysteine conserved among all eukaryotes.

Keyword(s): ATP-Binding Cassette Transporters: chemistry (MeSH) ; ATP-Binding Cassette Transporters: genetics (MeSH) ; ATP-Binding Cassette Transporters: metabolism (MeSH) ; Amino Acid Sequence (MeSH) ; Cysteine: chemistry (MeSH) ; Cysteine: metabolism (MeSH) ; Electron Spin Resonance Spectroscopy (MeSH) ; Evolution, Molecular (MeSH) ; Ferredoxins: chemistry (MeSH) ; Ferredoxins: metabolism (MeSH) ; Genetic Complementation Test (MeSH) ; Iron: chemistry (MeSH) ; Iron-Sulfur Proteins: chemistry (MeSH) ; Iron-Sulfur Proteins: genetics (MeSH) ; Iron-Sulfur Proteins: metabolism (MeSH) ; Molecular Sequence Data (MeSH) ; Mutagenesis, Site-Directed (MeSH) ; Saccharomyces cerevisiae (MeSH) ; Sequence Homology, Amino Acid (MeSH) ; Spectrophotometry, Ultraviolet (MeSH) ; Spectroscopy, Mossbauer (MeSH) ; Sulfolobus solfataricus: genetics (MeSH) ; Sulfolobus solfataricus: metabolism (MeSH) ; Sulfur: chemistry (MeSH) ; Ferredoxins ; Iron-Sulfur Proteins ; Cysteine ; Iron ; Sulfur

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Contributing Institute(s):

1. Experiments with synchrotron radiation (HASYLAB)
2. European Molecular Biology Laboratory (EMBL)

Research Program(s):

1. FS Beamline without reference (POF1-550) (POF1-550)

Experiment(s):

1. Unknown DESY Beamline

Appears in the scientific report 2007
Notes: Copyright (c) 2007 by the American Society for Biochemistry and Molecular Biology.

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Database coverage:
; ; JCR ; No Author Disambiguation ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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