Interchangeability and distinct properties of bacterial Fe-S cluster assembly systems: functional replacement of the isc and suf operons in Escherichia coli with the nifSU-like operon from Helicobacter pylori
- PMID: 15496591
- DOI: 10.1093/jb/mvh104
Interchangeability and distinct properties of bacterial Fe-S cluster assembly systems: functional replacement of the isc and suf operons in Escherichia coli with the nifSU-like operon from Helicobacter pylori
Abstract
The assembly of iron-sulfur (Fe-S) clusters, a key step in the post-translational maturation of Fe-S proteins, is mediated by a complex apparatus. In E. coli, this process involves two independent systems called ISC and SUF encoded by the iscSUA-hscBA-fdx gene cluster and sufABCDSE operon, respectively. Another system, termed NIF (nifSU), is required for the maturation of nitrogenase in nitrogen-fixing bacteria. We have developed a novel genetic system to gain further insight into these multi-component systems, and to determine how ISC, SUF and NIF might differ in their roles in Fe-S assembly. We have constructed an E. coli mutant lacking both the isc and suf operons, and this strain can only survive in the presence of a complementing plasmid. Using the plasmid replacement technique, we examined the isc and suf operons, and identified the genes essential for the function. Additionally, we have found that nifSU-like genes cloned from Helicobacter pylori are functionally exchangeable with the isc and suf operons. Thus, the NIF-like system participates in the maturation of a wide variety of Fe-S proteins. An increased ability of NIF to complement isc and suf loss was seen under anaerobic conditions. This may explain why the NIF system is only found in a limited number of bacterial species, and most other organisms prefer the ISC and/or SUF systems. While the differences between ISC and SUF were small with respect to the complementing activity, the SUF system appears to be more advantageous for bacterial growth in the presence of hydrogen peroxide.
Similar articles
-
How Escherichia coli and Saccharomyces cerevisiae build Fe/S proteins.Adv Microb Physiol. 2005;50:41-101. doi: 10.1016/S0065-2911(05)50002-X. Adv Microb Physiol. 2005. PMID: 16221578
-
A suf operon requirement for Fe-S cluster assembly during iron starvation in Escherichia coli.Mol Microbiol. 2004 May;52(3):861-72. doi: 10.1111/j.1365-2958.2004.04025.x. Mol Microbiol. 2004. PMID: 15101990
-
IscR acts as an activator in response to oxidative stress for the suf operon encoding Fe-S assembly proteins.Mol Microbiol. 2006 Jul;61(1):206-18. doi: 10.1111/j.1365-2958.2006.05220.x. Mol Microbiol. 2006. PMID: 16824106
-
Iron-sulfur cluster biogenesis systems and their crosstalk.Chembiochem. 2008 Oct 13;9(15):2355-62. doi: 10.1002/cbic.200800384. Chembiochem. 2008. PMID: 18798211 Review.
-
Recent advances in the Suf Fe-S cluster biogenesis pathway: Beyond the Proteobacteria.Biochim Biophys Acta. 2015 Jun;1853(6):1464-9. doi: 10.1016/j.bbamcr.2014.11.001. Epub 2014 Nov 7. Biochim Biophys Acta. 2015. PMID: 25447545 Free PMC article. Review.
Cited by
-
Small RNA-induced differential degradation of the polycistronic mRNA iscRSUA.EMBO J. 2009 Jun 3;28(11):1551-61. doi: 10.1038/emboj.2009.116. Epub 2009 Apr 30. EMBO J. 2009. PMID: 19407815 Free PMC article.
-
The Pneumococcal Protein SufC Binds to Host Plasminogen and Promotes Its Conversion into Plasmin.Microorganisms. 2023 Dec 12;11(12):2969. doi: 10.3390/microorganisms11122969. Microorganisms. 2023. PMID: 38138113 Free PMC article.
-
Building Fe-S proteins: bacterial strategies.Nat Rev Microbiol. 2010 Jun;8(6):436-46. doi: 10.1038/nrmicro2356. Nat Rev Microbiol. 2010. PMID: 20467446 Review.
-
Inferring gene function from evolutionary change in signatures of translation efficiency.Genome Biol. 2014 Mar 3;15(3):R44. doi: 10.1186/gb-2014-15-3-r44. Genome Biol. 2014. PMID: 24580753 Free PMC article.
-
Fe-S cluster assembly pathways in bacteria.Microbiol Mol Biol Rev. 2008 Mar;72(1):110-25, table of contents. doi: 10.1128/MMBR.00034-07. Microbiol Mol Biol Rev. 2008. PMID: 18322036 Free PMC article. Review.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Molecular Biology Databases
Miscellaneous