A fusion of the Bacteroides fragilis ferrous iron import proteins reveals a role for FeoA in stabilizing GTP-bound FeoB
Iron is an essential element for nearly all organisms, and under anoxic and/or reducing conditions, Fe2+ is the dominant form of iron available to bacteria. The ferrous iron transport (Feo) system is the primary prokaryotic Fe2+ import machinery, and two constituent proteins (FeoA and FeoB) are cons...
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Published in | The Journal of biological chemistry Vol. 298; no. 4; p. 101808 |
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Main Authors | , , , , , , |
Format | Journal Article |
Language | English |
Published |
United States
Elsevier Inc
01.04.2022
American Society for Biochemistry and Molecular Biology |
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Abstract | Iron is an essential element for nearly all organisms, and under anoxic and/or reducing conditions, Fe2+ is the dominant form of iron available to bacteria. The ferrous iron transport (Feo) system is the primary prokaryotic Fe2+ import machinery, and two constituent proteins (FeoA and FeoB) are conserved across most bacterial species. However, how FeoA and FeoB function relative to one another remains enigmatic. In this work, we explored the distribution of feoAB operons encoding a fusion of FeoA tethered to the N-terminal, G-protein domain of FeoB via a connecting linker region. We hypothesized that this fusion poises FeoA to interact with FeoB to affect function. To test this hypothesis, we characterized the soluble NFeoAB fusion protein from Bacteroides fragilis, a commensal organism implicated in drug-resistant infections. Using X-ray crystallography, we determined the 1.50-Å resolution structure of BfFeoA, which adopts an SH3-like fold implicated in protein–protein interactions. Using a combination of structural modeling, small-angle X-ray scattering, and hydrogen–deuterium exchange mass spectrometry, we show that FeoA and NFeoB interact in a nucleotide-dependent manner, and we mapped the protein–protein interaction interface. Finally, using guanosine triphosphate (GTP) hydrolysis assays, we demonstrate that BfNFeoAB exhibits one of the slowest known rates of Feo-mediated GTP hydrolysis that is not potassium-stimulated. Importantly, truncation of FeoA from this fusion demonstrates that FeoA–NFeoB interactions function to stabilize the GTP-bound form of FeoB. Taken together, our work reveals a role for FeoA function in the fused FeoAB system and suggests a function for FeoA among prokaryotes. |
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AbstractList | Iron is an essential element for nearly all organisms, and under anoxic and/or reducing conditions, Fe2+ is the dominant form of iron available to bacteria. The ferrous iron transport (Feo) system is the primary prokaryotic Fe2+ import machinery, and two constituent proteins (FeoA and FeoB) are conserved across most bacterial species. However, how FeoA and FeoB function relative to one another remains enigmatic. In this work, we explored the distribution of feoAB operons encoding a fusion of FeoA tethered to the N-terminal, G-protein domain of FeoB via a connecting linker region. We hypothesized that this fusion poises FeoA to interact with FeoB to affect function. To test this hypothesis, we characterized the soluble NFeoAB fusion protein from Bacteroides fragilis, a commensal organism implicated in drug-resistant infections. Using X-ray crystallography, we determined the 1.50-Å resolution structure of BfFeoA, which adopts an SH3-like fold implicated in protein–protein interactions. Using a combination of structural modeling, small-angle X-ray scattering, and hydrogen–deuterium exchange mass spectrometry, we show that FeoA and NFeoB interact in a nucleotide-dependent manner, and we mapped the protein–protein interaction interface. Finally, using guanosine triphosphate (GTP) hydrolysis assays, we demonstrate that BfNFeoAB exhibits one of the slowest known rates of Feo-mediated GTP hydrolysis that is not potassium-stimulated. Importantly, truncation of FeoA from this fusion demonstrates that FeoA–NFeoB interactions function to stabilize the GTP-bound form of FeoB. Taken together, our work reveals a role for FeoA function in the fused FeoAB system and suggests a function for FeoA among prokaryotes. Iron is an essential element for nearly all organisms, and under anoxic and/or reducing conditions, Fe is the dominant form of iron available to bacteria. The ferrous iron transport (Feo) system is the primary prokaryotic Fe import machinery, and two constituent proteins (FeoA and FeoB) are conserved across most bacterial species. However, how FeoA and FeoB function relative to one another remains enigmatic. In this work, we explored the distribution of feoAB operons encoding a fusion of FeoA tethered to the N-terminal, G-protein domain of FeoB via a connecting linker region. We hypothesized that this fusion poises FeoA to interact with FeoB to affect function. To test this hypothesis, we characterized the soluble NFeoAB fusion protein from Bacteroides fragilis, a commensal organism implicated in drug-resistant infections. Using X-ray crystallography, we determined the 1.50-Å resolution structure of BfFeoA, which adopts an SH3-like fold implicated in protein-protein interactions. Using a combination of structural modeling, small-angle X-ray scattering, and hydrogen-deuterium exchange mass spectrometry, we show that FeoA and NFeoB interact in a nucleotide-dependent manner, and we mapped the protein-protein interaction interface. Finally, using guanosine triphosphate (GTP) hydrolysis assays, we demonstrate that BfNFeoAB exhibits one of the slowest known rates of Feo-mediated GTP hydrolysis that is not potassium-stimulated. Importantly, truncation of FeoA from this fusion demonstrates that FeoA-NFeoB interactions function to stabilize the GTP-bound form of FeoB. Taken together, our work reveals a role for FeoA function in the fused FeoAB system and suggests a function for FeoA among prokaryotes. Iron is an essential element for nearly all organisms, and under anoxic and/or reducing conditions, Fe 2+ is the dominant form of iron available to bacteria. The ferrous iron transport (Feo) system is the primary prokaryotic Fe 2+ import machinery, and two constituent proteins (FeoA and FeoB) are conserved across most bacterial species. However, how FeoA and FeoB function relative to one another remains enigmatic. In this work, we explored the distribution of feoAB operons encoding a fusion of FeoA tethered to the N-terminal, G-protein domain of FeoB via a connecting linker region. We hypothesized that this fusion poises FeoA to interact with FeoB to affect function. To test this hypothesis, we characterized the soluble NFeoAB fusion protein from Bacteroides fragilis , a commensal organism implicated in drug-resistant infections. Using X-ray crystallography, we determined the 1.50-Å resolution structure of Bf FeoA, which adopts an SH3-like fold implicated in protein–protein interactions. Using a combination of structural modeling, small-angle X-ray scattering, and hydrogen–deuterium exchange mass spectrometry, we show that FeoA and NFeoB interact in a nucleotide-dependent manner, and we mapped the protein–protein interaction interface. Finally, using guanosine triphosphate (GTP) hydrolysis assays, we demonstrate that Bf NFeoAB exhibits one of the slowest known rates of Feo-mediated GTP hydrolysis that is not potassium-stimulated. Importantly, truncation of FeoA from this fusion demonstrates that FeoA–NFeoB interactions function to stabilize the GTP-bound form of FeoB. Taken together, our work reveals a role for FeoA function in the fused FeoAB system and suggests a function for FeoA among prokaryotes. |
ArticleNumber | 101808 |
Author | Deredge, Daniel J. Sestok, Alex E. Brown, Janae B. Smith, Aaron T. O’Sullivan, Sean M. Obi, Juliet O. Garcin, Elsa D. |
Author_xml | – sequence: 1 givenname: Alex E. surname: Sestok fullname: Sestok, Alex E. organization: Department of Chemistry and Biochemistry, University of Maryland, Baltimore County, Baltimore, Maryland, USA – sequence: 2 givenname: Janae B. surname: Brown fullname: Brown, Janae B. organization: Department of Chemistry and Biochemistry, University of Maryland, Baltimore County, Baltimore, Maryland, USA – sequence: 3 givenname: Juliet O. orcidid: 0000-0002-6851-0096 surname: Obi fullname: Obi, Juliet O. organization: Department of Pharmaceutical Sciences, University of Maryland School of Pharmacy, Baltimore, Maryland, USA – sequence: 4 givenname: Sean M. surname: O’Sullivan fullname: O’Sullivan, Sean M. organization: Department of Chemistry and Biochemistry, University of Maryland, Baltimore County, Baltimore, Maryland, USA – sequence: 5 givenname: Elsa D. orcidid: 0000-0003-0501-8421 surname: Garcin fullname: Garcin, Elsa D. organization: Department of Chemistry and Biochemistry, University of Maryland, Baltimore County, Baltimore, Maryland, USA – sequence: 6 givenname: Daniel J. surname: Deredge fullname: Deredge, Daniel J. organization: Department of Pharmaceutical Sciences, University of Maryland School of Pharmacy, Baltimore, Maryland, USA – sequence: 7 givenname: Aaron T. orcidid: 0000-0002-9332-8683 surname: Smith fullname: Smith, Aaron T. email: smitha@umbc.edu organization: Department of Chemistry and Biochemistry, University of Maryland, Baltimore County, Baltimore, Maryland, USA |
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Keywords | protein–protein interactions SEC-SAXS GTP IMAC TEV NFeoAB RMSD NFeoB SAXS Tris SEC Feo SDS-PAGE GDP NMR GMP-PNP IPTG iron iron transport TCEP SH3 |
Language | English |
License | This is an open access article under the CC BY license. Copyright © 2022 The Authors. Published by Elsevier Inc. All rights reserved. Attribution: http://creativecommons.org/licenses/by This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). |
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Snippet | Iron is an essential element for nearly all organisms, and under anoxic and/or reducing conditions, Fe2+ is the dominant form of iron available to bacteria.... Iron is an essential element for nearly all organisms, and under anoxic and/or reducing conditions, Fe is the dominant form of iron available to bacteria. The... Iron is an essential element for nearly all organisms, and under anoxic and/or reducing conditions, Fe 2+ is the dominant form of iron available to bacteria.... |
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SubjectTerms | Bacterial Proteins - chemistry Bacterial Proteins - metabolism Bacteroides fragilis - genetics Bacteroides fragilis - metabolism BASIC BIOLOGICAL SCIENCES Biochemistry, Molecular Biology Biophysics Cation Transport Proteins - metabolism Crystallography, X-Ray Feo Guanosine Triphosphate - chemistry Guanosine Triphosphate - metabolism Hydrolysis INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY iron Iron - metabolism iron transport Iron-Binding Proteins - chemistry Iron-Binding Proteins - metabolism Life Sciences Protein Stability protein–protein interactions SAXS SH3 |
Title | A fusion of the Bacteroides fragilis ferrous iron import proteins reveals a role for FeoA in stabilizing GTP-bound FeoB |
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