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Bacterial magnetosome biomineralization--a novel platform to study molecular mechanisms of human CDF-related Type-II diabetes.

Authors
  • 1
  • 2
  • 3
  • 1
  • 4
  • 2
  • 3
  • 4
  • 2
  • 1
  • 1 Department of Life Sciences, Ben Gurion University of the Negev, Beer-Sheva, Israel; The National Institute for Biotechnology in the Negev, Ben Gurion University of the Negev, Beer-Sheva, Israel. , (Israel)
  • 2 Ludwig Maximillian University of Munich, Dept. Biology I, Martinsried, Germany. , (Germany)
  • 3 Institute of Chemistry, The Hebrew University of Jerusalem, Givat Ram, Jerusalem, Israel. , (Israel)
  • 4 Department of Chemistry, Ben Gurion University of the Negev, Beer-Sheva, Israel; Ilse Katz Institute for Nanoscale Science and Technology, Ben-Gurion University of the Negev, Beer-Sheva, Israel. , (Israel)
Type
Published Article
Journal
PLoS ONE
1932-6203
Publisher
Public Library of Science
Publication Date
Volume
9
Issue
5
Identifiers
DOI: 10.1371/journal.pone.0097154
PMID: 24819161
Source
Medline
License
Unknown

Abstract

Cation diffusion facilitators (CDF) are part of a highly conserved protein family that maintains cellular divalent cation homeostasis in all organisms. CDFs were found to be involved in numerous human health conditions, such as Type-II diabetes and neurodegenerative diseases. In this work, we established the magnetite biomineralizing alphaproteobacterium Magnetospirillum gryphiswaldense as an effective model system to study CDF-related Type-II diabetes. Here, we introduced two ZnT-8 Type-II diabetes-related mutations into the M. gryphiswaldense MamM protein, a magnetosome-associated CDF transporter essential for magnetite biomineralization within magnetosome vesicles. The mutations' effects on magnetite biomineralization and iron transport within magnetosome vesicles were tested in vivo. Additionally, by combining several in vitro and in silico methodologies we provide new mechanistic insights for ZnT-8 polymorphism at position 325, located at a crucial dimerization site important for CDF regulation and activation. Overall, by following differentiated, easily measurable, magnetism-related phenotypes we can utilize magnetotactic bacteria for future research of CDF-related human diseases.

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