Iron Regulatory Proteins
Iron Regulatory Proteins - Related Videos
02:02
Cis-regulatory Sequences
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2020
Cis-regulatory sequences are short fragments of non-coding DNA that are present on the same chromosomes as the genes that they regulate. These fragments serve as binding sites for transcriptional regulators, proteins that are responsible for controlling gene transcription and differential gene expression across cell types in eukaryotes. Cis-regulatory sequences can be close to the gene of interest or thousands of bases away in the DNA sequence; however, those sequences that are further away are...
08:45
Quantitating Iron Transport Across the Mouse Placenta In Vivo Using Nonradioactive Iron Isotopes
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Cited by 3 •
2022
This article demonstrates how to prepare and administer transferrin-bound nonradioactive isotopic iron for studies of iron transport in mouse pregnancy. The approach for quantifying isotopic iron in fetoplacental compartments is also described.
06:37
Staphylococcus aureus Growth using Human Hemoglobin as an Iron Source
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Cited by 31 •
2013
Here we describe a growth assay for Staphylococcus aureus using hemoglobin as the sole source of available nutrient iron. This assay establishes the role of bacterial factors involved in hemoglobin-derived iron acquisition.
03:06
Culturing Mycobacterium tuberculosis Under Iron-Limited Conditions
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2025
Source: Gupta, S., et al. Isolation and Characterization of Extracellular Vesicles Produced by Iron-limited Mycobacteria. J. Vis. Exp. (2019)This video demonstrates the procedure for culturing Mycobacterium tuberculosis under iron-limited conditions to induce iron stress and promote the secretion of siderophores that support bacterial survival.
05:08
Measurement of Tissue Non-Heme Iron Content using a Bathophenanthroline-Based Colorimetric Assay
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Cited by 8 •
2022
Here, a protocol for the measurement of the non-heme iron content in animal tissues is provided, using a simple, well-established colorimetric assay that can be easily implemented in most laboratories.
FAQs
The location of the iron-responsive element, or IRE, determines which stage of gene expression IRP binding influences. An IRE in the 5′ untranslated region prevents ferritin messenger RNA from being translated, limiting iron storage. An IRE in the 3′ untranslated region instead stabilizes transferrin receptor messenger RNA, preserving the message needed for iron uptake.
The iron-sulfur cluster acts as a functional switch for IRP1. Under iron-rich conditions, IRP1 acquires the cluster and operates as aconitase rather than maintaining its RNA-binding regulatory role. This links cellular iron availability to a direct change in IRP1 activity, allowing the protein to shift between gene regulation and enzyme function.
IRP2 responds to increased iron through targeted degradation. As IRP2 is removed, its regulatory influence on iron-responsive messenger RNAs is released. This mechanism differs from IRP1, which changes function after acquiring an iron-sulfur cluster. Comparing both proteins shows that cells use distinct molecular strategies to adjust iron regulation as conditions change.
Ferritin and transferrin receptor control represent opposing requirements in cellular iron management. Repressing ferritin translation reduces iron storage, while stabilizing transferrin receptor messenger RNA promotes iron uptake. Examining both responses together reveals how IRPs coordinate iron acquisition with storage rather than regulating either process in isolation.
A useful comparison considers three linked outcomes: IRP binding to IRE-containing messenger RNAs, ferritin translation, and transferrin receptor messenger RNA stability. For IRP1, investigators can also assess the transition toward aconitase function after iron-sulfur cluster acquisition. Together, these observations distinguish regulatory activity from the iron-dependent functional states of the proteins.
IRP research connects molecular iron sensing with disorders in which iron balance is important, including anemia, neurodegeneration, infection, and other iron-related diseases. Examining how IRP1 and IRP2 alter ferritin production, transferrin receptor messenger RNA stability, or enzyme function can clarify how disrupted iron regulation contributes to disease mechanisms.