Sodium-Dependent Conformational Change in Flagellar Stator Protein MotS from Bacillus subtilis

Takekawa, Norihiro; Yamaguchi, Ayaka; Nishiuchi, Koki; Uehori, Maria; Kinoshita, Miki; Minamino, Tohru; Imada, Katsumi

doi:https://doi.org/10.3390/biom15020302

Sodium-Dependent Conformational Change in Flagellar Stator Protein MotS from Bacillus subtilis

Takekawa, Norihiro; Yamaguchi, Ayaka; Nishiuchi, Koki et al.

Biomolecules, 2025, 15(2), 302

Number of Access:563（2025-08-14 15:06 Counts）

Identifier to cite or link to this item: https://hdl.handle.net/11094/101060

Link to primary information

File	Format	Terms of use	Size	Views	Date.Available	Description	information
Biomolecules_15_2	pdf	None	2.83 MB	28	2025.04.21

Creative Commons : Attribution

Item Information

Output File Export EndNote Basic Export Mendeley

Title	Sodium-Dependent Conformational Change in Flagellar Stator Protein MotS from Bacillus subtilis
Creator	NRID 1000050791810 1000050791810 researchmap permalink takekawan takekawan Scopus Author ID 54416513800 54416513800 CreatorName Takekawa, Norihiro
	CreatorName Yamaguchi, Ayaka
	CreatorName Nishiuchi, Koki
	CreatorName Uehori, Maria
	NRID 1000030790985 1000030790985 researchmap permalink miki_kinoshita miki_kinoshita Scopus Author ID 35310858600 35310858600 CreatorName Kinoshita, Miki
	NRID 1000020402993 1000020402993 researchmap permalink tohru_minamino tohru_minamino Scopus Author ID 7006391123 7006391123 CreatorName Minamino, Tohru
	NRID 1000040346143 1000040346143 ORCID 0000-0003-1342-8885 0000-0003-1342-8885 researchmap permalink read0096832 read0096832 Scopus Author ID 7006628770 7006628770 CreatorName Imada, Katsumi
Subject	flagellum
	gram-positive bacteria
	stator
Description	Takekawa N., Yamaguchi A., Nishiuchi K., et al. Sodium-Dependent Conformational Change in Flagellar Stator Protein MotS from Bacillus subtilis. Biomolecules 15, 302 (2025); https://doi.org/10.3390/biom15020302.
Abstract	The bacterial flagellar motor consists of a rotor and stator units and is driven by ion flow through the stator. The activation of the ion flow is coupled with the anchoring of the stator units to the peptidoglycan layer by the stator B-subunit around the rotor. Gram-negative bacteria, such as Salmonella and Vibrio, change the conformation of the N-terminal helix of the periplasmic domain of the B-subunit to anchor the stator units. However, a recent high-speed atomic force microscopic study has suggested that the periplasmic domain of MotS, the stator B-subunit of the sodium (Na+)-driven stator of Bacillus subtilis, a gram-positive bacterium, unfolds at low external Na+ concentrations and folds at high Na+ concentrations to anchor the stator units. Here, we report the crystal structures of MotS68–242, a periplasmic fragment of MotS, from B. subtilis at high and low Na+ concentrations. We also performed far-UV CD spectroscopic analysis of the wild-type MotS68–242 and MotS78–242 proteins and mutant variants of MotS68–242 under high and low Na+ concentrations and found that the N-terminal disordered region of MotS68–242 shows a Na+-dependent coil–helix transition. We propose a mechanism of the Na+-dependent structural transition of Bs-MotS to anchor the stator units.
Publisher	Multidisciplinary Digital Publishing Institute (MDPI)
Source Title	Biomolecules
Volume (Issue)	15(2)
Page	302
Date of Issued	2025-02-18
Language	English
Handle URL	https://hdl.handle.net/11094/101060
eISSN	2218273X
Relation.isIdenticalTo	DOI (Publisher Version) https://doi.org/10.3390/biom15020302
Access Rights	open access
CopyRight	This article is licensed under a Creative Commons Attribution 4.0 International License.
oaire:version	Version of Record
Category	学術雑誌論文 Journal Article

Resource Type	journal article
Local Type	Journal Article
DCMI Type	Text
DCTERMS.bibliographicCitation	Biomolecules. 2025, 15(2), p. 302
DC.title	Sodium-Dependent Conformational Change in Flagellar Stator Protein MotS from Bacillus subtilis
DC.creator	Takekawa, Norihiro
	Yamaguchi, Ayaka
	Nishiuchi, Koki
	Uehori, Maria
	Kinoshita, Miki
	Minamino, Tohru
	Imada, Katsumi
DC.publisher	Multidisciplinary Digital Publishing Institute (MDPI)
DC.language' scheme='DCTERMS.RFC1766	English
DC.type' scheme='DCTERMS.DCMIType	Text
DCTERMS.issued' scheme='DCTERMS.W3CDTF	2025-02-18
DC.identifier	https://doi.org/10.3390/biom15020302
DC.subject	flagellum
	gram-positive bacteria
	stator
DC.description	Takekawa N., Yamaguchi A., Nishiuchi K., et al. Sodium-Dependent Conformational Change in Flagellar Stator Protein MotS from Bacillus subtilis. Biomolecules 15, 302 (2025); https://doi.org/10.3390/biom15020302.
DCTERMS.abstract	The bacterial flagellar motor consists of a rotor and stator units and is driven by ion flow through the stator. The activation of the ion flow is coupled with the anchoring of the stator units to the peptidoglycan layer by the stator B-subunit around the rotor. Gram-negative bacteria, such as Salmonella and Vibrio, change the conformation of the N-terminal helix of the periplasmic domain of the B-subunit to anchor the stator units. However, a recent high-speed atomic force microscopic study has suggested that the periplasmic domain of MotS, the stator B-subunit of the sodium (Na+)-driven stator of Bacillus subtilis, a gram-positive bacterium, unfolds at low external Na+ concentrations and folds at high Na+ concentrations to anchor the stator units. Here, we report the crystal structures of MotS68–242, a periplasmic fragment of MotS, from B. subtilis at high and low Na+ concentrations. We also performed far-UV CD spectroscopic analysis of the wild-type MotS68–242 and MotS78–242 proteins and mutant variants of MotS68–242 under high and low Na+ concentrations and found that the N-terminal disordered region of MotS68–242 shows a Na+-dependent coil–helix transition. We propose a mechanism of the Na+-dependent structural transition of Bs-MotS to anchor the stator units.
DC.rights	This article is licensed under a Creative Commons Attribution 4.0 International License.
DC.format	101060
citation_title	Sodium-Dependent Conformational Change in Flagellar Stator Protein MotS from Bacillus subtilis
citation_author	Takekawa, Norihiro
	Yamaguchi, Ayaka
	Nishiuchi, Koki
	Uehori, Maria
	Kinoshita, Miki
	Minamino, Tohru
	Imada, Katsumi
citation_publisher	Multidisciplinary Digital Publishing Institute (MDPI)
citation_language	English
citation_date	2025-02-18
citation_journal_title	Biomolecules
citation_volume	15
citation_issue	2
citation_firstpage	302
citation_doi	https://doi.org/10.3390/biom15020302
citation_public_url	https://hdl.handle.net/11094/101060

Sodium-Dependent Conformational Change in Flagellar Stator Protein MotS from Bacillus subtilis

Link to primary information

Item Information

Show details