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Manganese Oxide Nanoparticle Synthesis by Thermal Decomposition of ManganeseII Acetylacetonate
Published on: June 18, 2020
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Structure-function analysis of manganese exporter proteins across bacteria
Rilee Zeinert1, Eli Martinez1, Jennifer Schmitz1
1From the Department of Chemistry, University of Wisconsin, Oshkosh, Wisconsin 54901 and.
The Journal of Biological Chemistry
|February 15, 2018
Summary
This study reveals novel bacterial manganese transporters, MntP and UPF0016, crucial for cellular defense against oxidative stress and manganese export. It also identifies Alx as a protein that increases intracellular manganese levels.
Area of Science:
- Microbiology
- Biochemistry
- Molecular Biology
Background:
- Manganese (Mn) is essential for enzymes and reactive oxygen species (ROS) defense in organisms.
- Excess manganese is toxic, necessitating bacterial export mechanisms.
- Known manganese transporters (MntP, MntE) are insufficient to explain all transport.
Purpose of the Study:
- To characterize manganese transport proteins from MntP, UPF0016, and TerC families.
- To understand the function and structure of MntP in manganese homeostasis.
- To identify novel bacterial manganese transporters and their mechanisms.
Main Methods:
- Computational analysis (phylogeny, structure)
- Physiological assays (manganese/ROS sensitivity)
- Inductively coupled plasma-mass spectrometry (ICP-MS) for metal quantification
Main Results:
- MntP protein influences cellular resistance to ROS.
- Specific negatively charged amino acids are critical for MntP activity.
- UPF0016 family proteins exhibit manganese export activity.
- Alx (TerC family) increases intracellular manganese, unlike typical exporters.
Conclusions:
- MntP and UPF0016 proteins are key players in bacterial manganese homeostasis and ROS defense.
- Alx protein has a unique role in modulating intracellular manganese levels.
- Mn-responsive riboswitches can help identify novel manganese transport components.
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