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Disease-Homologous Mutation in the Cation Diffusion Facilitator Protein MamM Causes Single-Domain Structural Loss and Signifies Its Importance.

Title data

Barber-Zucker, Shiran ; Uebe, René ; Davidov, Geula ; Navon, Yotam ; Sherf, Dror ; Chill, Jordan H. ; Kass, Itamar ; Bitton, Ronit ; Schüler, Dirk ; Zarivach, Raz:
Disease-Homologous Mutation in the Cation Diffusion Facilitator Protein MamM Causes Single-Domain Structural Loss and Signifies Its Importance.
In: Scientific Reports. Vol. 6 (23 August 2016) . - No. 31933.
ISSN 2045-2322
DOI: https://doi.org/10.1038/srep31933

Abstract in another language

Cation diffusion facilitators (CDF) are highly conserved, metal ion efflux transporters that maintain divalent transition metal cation homeostasis. Most CDF proteins contain two domains, the cation transporting transmembrane domain and the regulatory cytoplasmic C-terminal domain (CTD). MamM is a magnetosome-associated CDF protein essential for the biomineralization of magnetic iron-oxide particles in magnetotactic bacteria. To investigate the structure-function relationship of CDF cytoplasmic domains, we characterized a MamM M250P mutation that is synonymous with the disease-related mutation L349P of the human CDF protein ZnT-10. Our results show that the M250P exchange in MamM causes severe structural changes in its CTD resulting in abnormal reduced function. Our in vivo, in vitro and in silico studies indicate that the CTD fold is critical for CDF proteins’ proper function and support the previously suggested role of the CDF cytoplasmic domain as a CDF regulatory element. Based on our results, we also suggest a mechanism for the effects of the ZnT-10 L349P mutation in human.

Further data

Item Type: Article in a journal
Refereed: Yes
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Biology > Chair Microbiology
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Biology > Chair Microbiology > Chair Microbiology - Univ.-Prof. Dr. Dirk Schüler
Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Biology
Result of work at the UBT: Yes
DDC Subjects: 500 Science > 500 Natural sciences
500 Science > 570 Life sciences, biology
Date Deposited: 23 Nov 2016 08:03
Last Modified: 09 Apr 2019 07:30
URI: https://eref.uni-bayreuth.de/id/eprint/35199