| Title: |
Structural organization of essential iron-sulfur clusters in the evolutionarily highly conserved ATP-binding cassette protein ABCE1 |
| Authors: |
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. |
| Source: |
The journal of biological chemistry 282, 14598-14607 (2007). doi:10.1074/jbc.M700825200 |
| Publisher Information: |
Soc. |
| Publication Year: |
2007 |
| Collection: |
DESY Publication Database (PUBDB) |
| Subject Terms: |
info:eu-repo/classification/ddc/570; ATP-Binding Cassette Transporters: chemistry; ATP-Binding Cassette Transporters: genetics; ATP-Binding Cassette Transporters: metabolism; Amino Acid Sequence; Cysteine: chemistry; Cysteine: metabolism; Electron Spin Resonance Spectroscopy; Evolution; Molecular; Ferredoxins: chemistry; Ferredoxins: metabolism; Genetic Complementation Test; Iron: chemistry; Iron-Sulfur Proteins: chemistry; Iron-Sulfur Proteins: genetics; Iron-Sulfur Proteins: metabolism; Molecular Sequence Data; Mutagenesis; Site-Directed; Saccharomyces cerevisiae; Sequence Homology; Amino Acid; Spectrophotometry; Ultraviolet; Spectroscopy; Mossbauer; Sulfolobus solfataricus: genetics; Sulfolobus solfataricus: metabolism; Sulfur: chemistry |
| Subject Geographic: |
DE |
| Description: |
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. |
| Document Type: |
article in journal/newspaper |
| Language: |
English |
| ISSN: |
0021-9258; 1083-351X |
| Relation: |
info:eu-repo/semantics/altIdentifier/wos/WOS:000246245800073; info:eu-repo/semantics/altIdentifier/issn/0021-9258; info:eu-repo/semantics/altIdentifier/pmid/pmid:17355973; info:eu-repo/semantics/altIdentifier/issn/1083-351X |
| Availability: |
https://bib-pubdb1.desy.de/record/83909; https://bib-pubdb1.desy.de/search?p=id:%22PHPPUBDB-4359%22 |
| Rights: |
info:eu-repo/semantics/openAccess |
| Accession Number: |
edsbas.CD1F07BC |
| Database: |
BASE |