Biochemical and structural characterization of a thermostable Dps protein with His‐type ferroxidase centers and outer metal‐binding sites

The DNA‐binding protein from starved cells (Dps) is found in a wide range of microorganisms, and it has been well characterized. However, little is known about Dps proteins from nonheterocystous filamentous cyanobacteria. In this study, a Dps protein from the thermophilic nonheterocystous filamentou...

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Autores principales: Minato, Takuo, Teramoto, Takamasa, Kakuta, Yoshimitsu, Ogo, Seiji, Yoon, Ki‐Seok
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2020
Materias:
Research Articles
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7327923/
https://www.ncbi.nlm.nih.gov/pubmed/32170832
http://dx.doi.org/10.1002/2211-5463.12837
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author Minato, Takuo
Teramoto, Takamasa
Kakuta, Yoshimitsu
Ogo, Seiji
Yoon, Ki‐Seok
author_facet Minato, Takuo
Teramoto, Takamasa
Kakuta, Yoshimitsu
Ogo, Seiji
Yoon, Ki‐Seok
author_sort Minato, Takuo
collection PubMed
description The DNA‐binding protein from starved cells (Dps) is found in a wide range of microorganisms, and it has been well characterized. However, little is known about Dps proteins from nonheterocystous filamentous cyanobacteria. In this study, a Dps protein from the thermophilic nonheterocystous filamentous cyanobacterium Thermoleptolyngbya sp. O‐77 (TlDps1) was purified and characterized. PAGE and CD analyses of TlDps1 demonstrated that it had higher thermostability than previously reported Dps proteins. X‐ray crystallographic analysis revealed that TlDps1 possessed His‐type ferroxidase centers within the cavity and unique metal‐binding sites located on the surface of the protein, which presumably contributed to its exceedingly high thermostability.
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spelling pubmed-73279232020-07-02 Biochemical and structural characterization of a thermostable Dps protein with His‐type ferroxidase centers and outer metal‐binding sites Minato, Takuo Teramoto, Takamasa Kakuta, Yoshimitsu Ogo, Seiji Yoon, Ki‐Seok FEBS Open Bio Research Articles The DNA‐binding protein from starved cells (Dps) is found in a wide range of microorganisms, and it has been well characterized. However, little is known about Dps proteins from nonheterocystous filamentous cyanobacteria. In this study, a Dps protein from the thermophilic nonheterocystous filamentous cyanobacterium Thermoleptolyngbya sp. O‐77 (TlDps1) was purified and characterized. PAGE and CD analyses of TlDps1 demonstrated that it had higher thermostability than previously reported Dps proteins. X‐ray crystallographic analysis revealed that TlDps1 possessed His‐type ferroxidase centers within the cavity and unique metal‐binding sites located on the surface of the protein, which presumably contributed to its exceedingly high thermostability. John Wiley and Sons Inc. 2020-05-28 /pmc/articles/PMC7327923/ /pubmed/32170832 http://dx.doi.org/10.1002/2211-5463.12837 Text en © 2020 The Authors. Published by FEBS Press and John Wiley & Sons Ltd. This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Articles
Minato, Takuo
Teramoto, Takamasa
Kakuta, Yoshimitsu
Ogo, Seiji
Yoon, Ki‐Seok
Biochemical and structural characterization of a thermostable Dps protein with His‐type ferroxidase centers and outer metal‐binding sites
title Biochemical and structural characterization of a thermostable Dps protein with His‐type ferroxidase centers and outer metal‐binding sites
title_full Biochemical and structural characterization of a thermostable Dps protein with His‐type ferroxidase centers and outer metal‐binding sites
title_fullStr Biochemical and structural characterization of a thermostable Dps protein with His‐type ferroxidase centers and outer metal‐binding sites
title_full_unstemmed Biochemical and structural characterization of a thermostable Dps protein with His‐type ferroxidase centers and outer metal‐binding sites
title_short Biochemical and structural characterization of a thermostable Dps protein with His‐type ferroxidase centers and outer metal‐binding sites
title_sort biochemical and structural characterization of a thermostable dps protein with his‐type ferroxidase centers and outer metal‐binding sites
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7327923/
https://www.ncbi.nlm.nih.gov/pubmed/32170832
http://dx.doi.org/10.1002/2211-5463.12837
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