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Main Authors: Lara-Gutiérrez, Juanita, Nguyen, Jen, McIlvin, Matthew R, Sugiyama, Ichiko, Landry, Zachary C, Alcolombri, Uria, Pontrelli, Sammy, Jiménez-Martínez, Joaquín, Sauer, Uwe, Hwa, Terence, Keegstra, Johannes M, Saito, Mak A, Stocker, Roman
Format: Artículo científico
Language:en
Published: Proceedings of the National Academy of Sciences of the United States of America 2026
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Online Access:https://pubmed.ncbi.nlm.nih.gov/41671182/
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author Lara-Gutiérrez, Juanita
Nguyen, Jen
McIlvin, Matthew R
Sugiyama, Ichiko
Landry, Zachary C
Alcolombri, Uria
Pontrelli, Sammy
Jiménez-Martínez, Joaquín
Sauer, Uwe
Hwa, Terence
Keegstra, Johannes M
Saito, Mak A
Stocker, Roman
author_facet Lara-Gutiérrez, Juanita
Nguyen, Jen
McIlvin, Matthew R
Sugiyama, Ichiko
Landry, Zachary C
Alcolombri, Uria
Pontrelli, Sammy
Jiménez-Martínez, Joaquín
Sauer, Uwe
Hwa, Terence
Keegstra, Johannes M
Saito, Mak A
Stocker, Roman
Lara-Gutiérrez, Juanita
Nguyen, Jen
McIlvin, Matthew R
Sugiyama, Ichiko
Landry, Zachary C
Alcolombri, Uria
Pontrelli, Sammy
Jiménez-Martínez, Joaquín
Sauer, Uwe
Hwa, Terence
Keegstra, Johannes M
Saito, Mak A
Stocker, Roman
collection PubMed - marine biology
contents Bacterial iron acquisition by is facilitated by amino acid complexation in a rapid-renewal environment. Lara-Gutiérrez, Juanita Nguyen, Jen McIlvin, Matthew R Sugiyama, Ichiko Landry, Zachary C Alcolombri, Uria Pontrelli, Sammy Jiménez-Martínez, Joaquín Sauer, Uwe Hwa, Terence Keegstra, Johannes M Saito, Mak A Stocker, Roman Iron Amino Acids Escherichia coli Siderophores Histidine In natural environments, bacteria often encounter low concentrations of nutrient mixtures that are continuously replenished by physical processes such as fluid flow. Studying bacterial physiology under such conditions is experimentally challenging because it is difficult to maintain steady, low nutrient concentrations with rapid renewal. Most studies on nutrient limitation have used approaches such as the chemostat, which rely on long renewal times to sustain low concentrations. We developed a Millifluidic Continuous Culture Device (MCCD), inspired by microfluidics, that enables bacterial cultivation in nutrient mixtures at low micromolar concentrations with rapid renewal driven by fluid flow. Unlike microfluidic systems, the MCCD retains sufficient culture volume to support batch-scale 'omic analyses. Using the MCCD, we cultured in a mixture of amino acids and nucleobases at three concentration ranges spanning a fivefold difference in growth rates. Surprisingly, at the lowest concentration range, cells exhibited proteomic signatures of iron limitation despite equal total ferrous iron across conditions. Uptake experiments with labeled iron-histidine and iron-cysteine complexes confirmed that amino acids facilitated ferrous iron acquisition. Under continuous flow, siderophores were washed out, rendering this pathway ineffective and revealing a previously unrecognized mechanism of iron acquisition via soluble ferrous iron-amino acid complexes. These findings highlight the importance of studying bacterial physiology at low nutrient concentrations and also suggest a broader role for other organic substrates capable of complexing iron as potential iron sources in environments with rapid renewal.
format Artículo científico
id pubmed_41671182
institution PubMed
language en
publishDate 2026
publisher Proceedings of the National Academy of Sciences of the United States of America
record_format pubmed
spellingShingle Bacterial iron acquisition by is facilitated by amino acid complexation in a rapid-renewal environment.
Lara-Gutiérrez, Juanita
Nguyen, Jen
McIlvin, Matthew R
Sugiyama, Ichiko
Landry, Zachary C
Alcolombri, Uria
Pontrelli, Sammy
Jiménez-Martínez, Joaquín
Sauer, Uwe
Hwa, Terence
Keegstra, Johannes M
Saito, Mak A
Stocker, Roman
Iron
Amino Acids
Escherichia coli
Siderophores
Histidine
Bacterial iron acquisition by is facilitated by amino acid complexation in a rapid-renewal environment. Lara-Gutiérrez, Juanita Nguyen, Jen McIlvin, Matthew R Sugiyama, Ichiko Landry, Zachary C Alcolombri, Uria Pontrelli, Sammy Jiménez-Martínez, Joaquín Sauer, Uwe Hwa, Terence Keegstra, Johannes M Saito, Mak A Stocker, Roman Iron Amino Acids Escherichia coli Siderophores Histidine In natural environments, bacteria often encounter low concentrations of nutrient mixtures that are continuously replenished by physical processes such as fluid flow. Studying bacterial physiology under such conditions is experimentally challenging because it is difficult to maintain steady, low nutrient concentrations with rapid renewal. Most studies on nutrient limitation have used approaches such as the chemostat, which rely on long renewal times to sustain low concentrations. We developed a Millifluidic Continuous Culture Device (MCCD), inspired by microfluidics, that enables bacterial cultivation in nutrient mixtures at low micromolar concentrations with rapid renewal driven by fluid flow. Unlike microfluidic systems, the MCCD retains sufficient culture volume to support batch-scale 'omic analyses. Using the MCCD, we cultured in a mixture of amino acids and nucleobases at three concentration ranges spanning a fivefold difference in growth rates. Surprisingly, at the lowest concentration range, cells exhibited proteomic signatures of iron limitation despite equal total ferrous iron across conditions. Uptake experiments with labeled iron-histidine and iron-cysteine complexes confirmed that amino acids facilitated ferrous iron acquisition. Under continuous flow, siderophores were washed out, rendering this pathway ineffective and revealing a previously unrecognized mechanism of iron acquisition via soluble ferrous iron-amino acid complexes. These findings highlight the importance of studying bacterial physiology at low nutrient concentrations and also suggest a broader role for other organic substrates capable of complexing iron as potential iron sources in environments with rapid renewal.
title Bacterial iron acquisition by is facilitated by amino acid complexation in a rapid-renewal environment.
topic Iron
Amino Acids
Escherichia coli
Siderophores
Histidine
url https://pubmed.ncbi.nlm.nih.gov/41671182/