Vibrio cholerae FeoA, FeoB, and FeoC Interact To Form a Complex

Journal of Bacteriology
Begoña StevensonShelley M Payne

Abstract

Feo is the major ferrous iron transport system in prokaryotes. Despite having been discovered over 25 years ago and found to be widely distributed among bacteria, Feo is poorly understood, as its structure and mechanism of iron transport have not been determined. The feo operon in Vibrio cholerae is made up of three genes, encoding the FeoA, FeoB, and FeoC proteins, which are all required for Feo system function. FeoA and FeoC are both small cytoplasmic proteins, and their function remains unclear. FeoB, which is thought to function as a ferrous iron permease, is a large integral membrane protein made up of an N-terminal GTPase domain and a C-terminal membrane-spanning region. To date, structural studies of FeoB have been carried out using a truncated form of the protein encompassing only the N-terminal GTPase region. In this report, we show that full-length FeoB forms higher-order complexes when cross-linked in vivo in V. cholerae. Our analysis of these complexes revealed that FeoB can simultaneously associate with both FeoA and FeoC to form a large complex, an observation that has not been reported previously. We demonstrate that interactions between FeoB and FeoA, but not between FeoB and FeoC, are required for complex forma...Continue Reading

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Citations

May 15, 2016·Anaerobe·Milena M AwadJulian I Rood
Jun 29, 2018·Metallomics : Integrated Biometal Science·Alexandrea E SestokAaron T Smith
Aug 12, 2018·Applied and Environmental Microbiology·Lulu LiuHaichun Gao
Feb 15, 2019·Proceedings of the National Academy of Sciences of the United States of America·Minhye ShinShelley M Payne
Apr 20, 2017·Frontiers in Cellular and Infection Microbiology·Girija Ramakrishnan
Nov 12, 2020·Metallomics : Integrated Biometal Science·Camilo Gómez-Garzón, Shelley M Payne
Nov 13, 2019·Biochemistry·Aaron T SmithKelly N Chacón
Apr 29, 2020·ACS Central Science·Nathaniel P EndicottTimothy A Wencewicz

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