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A protein-protein interaction in magnetosomes: TPR protein MamA interacts with an Mms6 protein
Magnetosomes are membrane-enveloped bacterial organelles containing nano-sized magnetic particles, and function as a cellular magnetic sensor, which assist the cells to navigate and swim along the geomagnetic field. Localized with each magnetosome is a suite of proteins involved in the synthesis, ma...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5613248/ https://www.ncbi.nlm.nih.gov/pubmed/28955887 http://dx.doi.org/10.1016/j.bbrep.2016.05.010 |
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author | Nguyen, Hoang Viet Suzuki, Emi Oestreicher, Zachery Minamide, Hiroshi Endoh, Hiroshi Fukumori, Yoshihiro Taoka, Azuma |
author_facet | Nguyen, Hoang Viet Suzuki, Emi Oestreicher, Zachery Minamide, Hiroshi Endoh, Hiroshi Fukumori, Yoshihiro Taoka, Azuma |
author_sort | Nguyen, Hoang Viet |
collection | PubMed |
description | Magnetosomes are membrane-enveloped bacterial organelles containing nano-sized magnetic particles, and function as a cellular magnetic sensor, which assist the cells to navigate and swim along the geomagnetic field. Localized with each magnetosome is a suite of proteins involved in the synthesis, maintenance and functionalization of the organelle, however the detailed molecular organization of the proteins in magnetosomes is unresolved. MamA is one of the most abundant magnetosome-associated proteins and is anchored to the magnetosome vesicles through protein-protein interactions, but the identity of the protein that interacts with MamA is undetermined. In this study, we found that MamA binds to a magnetosome membrane protein Mms6. Two different molecular masses of Mms6, 14.5-kDa and 6.0-kDa, were associated with the magnetosomes. Using affinity chromatography, we identified that the 14.5-kDa Mms6 interacts with MamA, and the interaction was further confirmed by pull-down, immunoprecipitation and size-exclusion chromatography assays. Prior to this, Mms6 was assumed to be strictly involved with biomineralizing magnetite; however, these results suggest that Mms6 has an additional responsibility, binding to MamA. |
format | Online Article Text |
id | pubmed-5613248 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-56132482017-09-27 A protein-protein interaction in magnetosomes: TPR protein MamA interacts with an Mms6 protein Nguyen, Hoang Viet Suzuki, Emi Oestreicher, Zachery Minamide, Hiroshi Endoh, Hiroshi Fukumori, Yoshihiro Taoka, Azuma Biochem Biophys Rep Research Article Magnetosomes are membrane-enveloped bacterial organelles containing nano-sized magnetic particles, and function as a cellular magnetic sensor, which assist the cells to navigate and swim along the geomagnetic field. Localized with each magnetosome is a suite of proteins involved in the synthesis, maintenance and functionalization of the organelle, however the detailed molecular organization of the proteins in magnetosomes is unresolved. MamA is one of the most abundant magnetosome-associated proteins and is anchored to the magnetosome vesicles through protein-protein interactions, but the identity of the protein that interacts with MamA is undetermined. In this study, we found that MamA binds to a magnetosome membrane protein Mms6. Two different molecular masses of Mms6, 14.5-kDa and 6.0-kDa, were associated with the magnetosomes. Using affinity chromatography, we identified that the 14.5-kDa Mms6 interacts with MamA, and the interaction was further confirmed by pull-down, immunoprecipitation and size-exclusion chromatography assays. Prior to this, Mms6 was assumed to be strictly involved with biomineralizing magnetite; however, these results suggest that Mms6 has an additional responsibility, binding to MamA. Elsevier 2016-05-13 /pmc/articles/PMC5613248/ /pubmed/28955887 http://dx.doi.org/10.1016/j.bbrep.2016.05.010 Text en © 2016 The Authors http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Research Article Nguyen, Hoang Viet Suzuki, Emi Oestreicher, Zachery Minamide, Hiroshi Endoh, Hiroshi Fukumori, Yoshihiro Taoka, Azuma A protein-protein interaction in magnetosomes: TPR protein MamA interacts with an Mms6 protein |
title | A protein-protein interaction in magnetosomes: TPR protein MamA interacts with an Mms6 protein |
title_full | A protein-protein interaction in magnetosomes: TPR protein MamA interacts with an Mms6 protein |
title_fullStr | A protein-protein interaction in magnetosomes: TPR protein MamA interacts with an Mms6 protein |
title_full_unstemmed | A protein-protein interaction in magnetosomes: TPR protein MamA interacts with an Mms6 protein |
title_short | A protein-protein interaction in magnetosomes: TPR protein MamA interacts with an Mms6 protein |
title_sort | protein-protein interaction in magnetosomes: tpr protein mama interacts with an mms6 protein |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5613248/ https://www.ncbi.nlm.nih.gov/pubmed/28955887 http://dx.doi.org/10.1016/j.bbrep.2016.05.010 |
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