Bibliographic Details
| Title: |
Escherichia coli monothiol glutaredoxin GrxD replenishes Fe-S clusters to the essential ErpA A-type carrier under low iron stress. |
| Authors: |
Fisher, Claire E.1, Bak, Daniel W.2, Miller, Kennedy E.1, Washington-Hughes, Clorissa L.1, Dickfoss, Anna M.1, Weerapana, Eranthie2, Py, Béatrice3 py@imm.cnrs.fr, Outten, F. Wayne1 woutten@sc.edu |
| Source: |
Journal of Biological Chemistry. Aug2024, Vol. 300 Issue 8, p1-14. 14p. |
| Subject Terms: |
*ESCHERICHIA coli, *GLUTAREDOXIN, *MASS spectrometry, *BIOSYNTHESIS, *ISOPENTENOIDS |
| Abstract: |
Iron-sulfur (Fe-S) clusters are required for essential biological pathways, including respiration and isoprenoid biosynthesis. Complex Fe-S cluster biogenesis systems have evolved to maintain an adequate supply of this critical protein cofactor. In Escherichia coli, two Fe-S biosynthetic systems, the “housekeeping” Isc and “stress responsive” Suf pathways, interface with a network of cluster trafficking proteins, such as ErpA, IscA, SufA, and NfuA. GrxD, a Fe-S cluster-binding monothiol glutaredoxin, also participates in Fe-S protein biogenesis in both prokaryotes and eukaryotes. Previous studies in E. coli showed that the DgrxD mutation causes sensitivity to iron depletion, spotlighting a critical role for GrxD under conditions that disrupt Fe-S homeostasis. Here, we utilized a global chemoproteomic mass spectrometry approach to analyze the contribution of GrxD to the Fe-S proteome. Our results demonstrate that (1) GrxD is required for biogenesis of a specific subset of Fe-S proteins under iron-depleted conditions, (2) GrxD is required for cluster delivery to ErpA under iron limitation, (3) GrxD is functionally distinct from other Fe-S trafficking proteins, and (4) GrxD Fe-S cluster binding is responsive to iron limitation. All these results lead to the proposal that GrxD is required to maintain Fe-S cluster delivery to the essential trafficking protein ErpA during iron limitation conditions. [ABSTRACT FROM AUTHOR] |
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| Database: |
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