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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Frazzon, Jeverson Riboldi, Gustavo P. De Oliveira, Jaim S. |
| Description | Author Affiliation: Riboldi GP ( Federal University of Rio Grande do Sul, Porto Alegre, RS, Brazil.) |
| Abstract | Iron–sulfur [Fe–S] clusters are inorganic prosthetic groups that play essential roles in all living organisms. In vivo [Fe–S] cluster biogenesis requires enzymes involved in iron and sulfur mobilization, assembly of clusters, and delivery to their final acceptor. In these systems, a cysteine desulfurase is responsible for the release of sulfide ions, which are incorporated into a scaffold protein for subsequent [Fe–S] cluster assembly. Although three machineries have been shown to be present in Proteobacteria for [Fe–S] cluster biogenesis (NIF, ISC, and SUF), only the SUF machinery has been found in Firmicutes . We have recently described the structural similarities and differences between Enterococcus faecalis and Escherichia coli SufU proteins, which prompted the proposal that SufU is the scaffold protein of the E. faecalis suf CDSUB system. The present work aims at elucidating the biological roles of E. faecalis SufS and SufU proteins in [Fe–S] cluster assembly. We show that SufS has cysteine desulfurase activity and cysteine-365 plays an essential role in catalysis. SufS requires SufU as activator to [4Fe–4S] cluster assembly, as its ortholog, IscU, in which the conserved cysteine-153 acts as a proximal sulfur acceptor for transpersulfurization reaction. |
| ISSN | 00063002 |
| Journal | Biochimica et Biophysica Acta (BBA) - Reviews on Cancer |
| Issue Number | 12 |
| Volume Number | 1814 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2011-12-01 |
| Publisher Place | Netherlands |
| Access Restriction | Open |
| Subject Keyword | Carbon-Sulfur Lyases Metabolism Cysteine Enterococcus Faecalis Enzymology Iron-Sulfur Proteins Physiology Amino Acid Sequence Bacterial Proteins Chemistry Genetics Isolation & Purification Cloning, Molecular Enzyme Activation Models, Molecular Protein Binding Substrate Specificity Research Support, Non-U.S. Gov't Biochemistry |
| Content Type | Text |
| Resource Type | Article |
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