Structural similarities and differences in H-NS family proteins revealed by the N-terminal structure of TurB in Pseudomonas putida KT2440

Chiho Suzuki-Minakuchi; Kohei Kawazuma; Jun Matsuzawa; Delyana Vasileva; Zui Fujimoto; Tohru Terada; Kazunori Okada; Hideaki Nojiri

doi:10.1002/1873-3468.12425

Structural similarities and differences in H-NS family proteins revealed by the N-terminal structure of TurB in Pseudomonas putida KT2440

Chiho Suzuki-Minakuchi, Kohei Kawazuma, Jun Matsuzawa, Delyana Vasileva, Zui Fujimoto, Tohru Terada, Kazunori Okada, Hideaki Nojiri

Research output: Contribution to journal › Article › peer-review

9 Scopus citations

Abstract

H-NS family proteins play key roles in bacterial nucleoid compaction and global transcription. MvaT homologues in Pseudomonas have almost negligible amino acid sequence identity with H-NS, but can complement an hns-related phenotype of Escherichia coli. Here, we report the crystal structure of the N-terminal dimerization/oligomerization domain of TurB, an MvaT homologue in Pseudomonas putida KT2440. Our data identify two dimerization sites; the structure of the central dimerization site is almost the same as the corresponding region of H-NS, whereas the terminal dimerization sites are different. Our results reveal similarities and differences in dimerization and oligomerization mechanisms between H-NS and TurB.

Original language	English
Pages (from-to)	3583-3594
Number of pages	12
Journal	FEBS Letters
Volume	590
Issue number	20
DOIs	https://doi.org/10.1002/1873-3468.12425
State	Published - Oct 1 2016
Externally published	Yes

Funding

We thank Dr William Navarre from the University of Toronto for his comments in the preparation of the manuscript. This research was supported by the Platform Project for Supporting in Drug Discovery and Life Science Research (Platform for Drug Discovery, Informatics, and Structural Life Science, PDIS) from the Ministry of Education, Culture, Sports, Science and Technology (MEXT) and Japan Agency for Medical Research and Development (AMED) (Proposal No. 2023 and 2053). This work has been performed under the approval of the Photon Factory Program Advisory Committee (Proposal No. 2007G668 and 2011G595, as well as through PDIS). The synchrotron radiation experiments were also performed at BL26B1 in SPring-8 with the approval of the Japan Synchrotron Radiation Research Institute (JASRI) through PDIS. This study was also supported by Kato Memorial Bioscience Foundation (to CSM).

Funders	Funder number
Platform for Drug Discovery, Informatics, and Structural Life Science
Japan Agency for Medical Research and Development	2007G668, 2023, 2053, 2011G595
Japan Society for the Promotion of Science	15J10999
Ministry of Education, Culture, Sports, Science and Technology
Kato Memorial Bioscience Foundation

Keywords

H-NS
Pseudomonas
bacteria
crystal structure
nucleoid-associated protein
protein–protein interaction

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10.1002/1873-3468.12425

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title = "Structural similarities and differences in H-NS family proteins revealed by the N-terminal structure of TurB in Pseudomonas putida KT2440",

abstract = "H-NS family proteins play key roles in bacterial nucleoid compaction and global transcription. MvaT homologues in Pseudomonas have almost negligible amino acid sequence identity with H-NS, but can complement an hns-related phenotype of Escherichia coli. Here, we report the crystal structure of the N-terminal dimerization/oligomerization domain of TurB, an MvaT homologue in Pseudomonas putida KT2440. Our data identify two dimerization sites; the structure of the central dimerization site is almost the same as the corresponding region of H-NS, whereas the terminal dimerization sites are different. Our results reveal similarities and differences in dimerization and oligomerization mechanisms between H-NS and TurB.",

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author = "Chiho Suzuki-Minakuchi and Kohei Kawazuma and Jun Matsuzawa and Delyana Vasileva and Zui Fujimoto and Tohru Terada and Kazunori Okada and Hideaki Nojiri",

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AU - Suzuki-Minakuchi, Chiho

AU - Kawazuma, Kohei

AU - Matsuzawa, Jun

AU - Vasileva, Delyana

AU - Fujimoto, Zui

AU - Terada, Tohru

AU - Okada, Kazunori

AU - Nojiri, Hideaki

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AB - H-NS family proteins play key roles in bacterial nucleoid compaction and global transcription. MvaT homologues in Pseudomonas have almost negligible amino acid sequence identity with H-NS, but can complement an hns-related phenotype of Escherichia coli. Here, we report the crystal structure of the N-terminal dimerization/oligomerization domain of TurB, an MvaT homologue in Pseudomonas putida KT2440. Our data identify two dimerization sites; the structure of the central dimerization site is almost the same as the corresponding region of H-NS, whereas the terminal dimerization sites are different. Our results reveal similarities and differences in dimerization and oligomerization mechanisms between H-NS and TurB.

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KW - bacteria

KW - crystal structure

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Structural similarities and differences in H-NS family proteins revealed by the N-terminal structure of TurB in Pseudomonas putida KT2440

Abstract

Funding

Keywords

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