Structure and antimicrobial activity of NCR169, a nodule-specific cysteine-rich peptide of Medicago truncatula

Abstract A model legume, Medicago truncatula, has over 600 nodule-specific cysteine-rich (NCR) peptides required for symbiosis with rhizobia. Among them, NCR169, an essential factor for establishing symbiosis, has four cysteine residues that are indispensable for its function. However, knowledge of...

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Autores principales:	Noriyoshi Isozumi, Yuya Masubuchi, Tomohiro Imamura, Masashi Mori, Hironori Koga, Shinya Ohki
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/219e7e335d924fcd8a489737c3b2bfd9
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spelling	oai:doaj.org-article:219e7e335d924fcd8a489737c3b2bfd92021-12-02T15:36:13ZStructure and antimicrobial activity of NCR169, a nodule-specific cysteine-rich peptide of Medicago truncatula10.1038/s41598-021-89485-w2045-2322https://doaj.org/article/219e7e335d924fcd8a489737c3b2bfd92021-05-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-89485-whttps://doaj.org/toc/2045-2322Abstract A model legume, Medicago truncatula, has over 600 nodule-specific cysteine-rich (NCR) peptides required for symbiosis with rhizobia. Among them, NCR169, an essential factor for establishing symbiosis, has four cysteine residues that are indispensable for its function. However, knowledge of NCR169 structure and mechanism of action is still lacking. In this study, we solved two NMR structures of NCR169 caused by different disulfide linkage patterns. We show that both structures have a consensus C-terminal β-sheet attached to an extended N-terminal region with dissimilar features; one moves widely, whereas the other is relatively stapled. We further revealed that the disulfide bonds of NCR169 contribute to its structural stability and solubility. Regarding the function, one of the NCR169 oxidized forms could bind to negatively charged bacterial phospholipids. Furthermore, the positively charged lysine-rich region of NCR169 may be responsible for its antimicrobial activity against Escherichia coli and Sinorhizobium meliloti. This active region was disordered even in the phospholipid bound state, suggesting that the disordered conformation of this region is key to its function. Morphological observations suggested the mechanism of action of NCR169 on bacteria. The present study on NCR169 provides new insights into the structure and function of NCR peptides.Noriyoshi IsozumiYuya MasubuchiTomohiro ImamuraMasashi MoriHironori KogaShinya OhkiNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-12 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Noriyoshi Isozumi Yuya Masubuchi Tomohiro Imamura Masashi Mori Hironori Koga Shinya Ohki Structure and antimicrobial activity of NCR169, a nodule-specific cysteine-rich peptide of Medicago truncatula
description	Abstract A model legume, Medicago truncatula, has over 600 nodule-specific cysteine-rich (NCR) peptides required for symbiosis with rhizobia. Among them, NCR169, an essential factor for establishing symbiosis, has four cysteine residues that are indispensable for its function. However, knowledge of NCR169 structure and mechanism of action is still lacking. In this study, we solved two NMR structures of NCR169 caused by different disulfide linkage patterns. We show that both structures have a consensus C-terminal β-sheet attached to an extended N-terminal region with dissimilar features; one moves widely, whereas the other is relatively stapled. We further revealed that the disulfide bonds of NCR169 contribute to its structural stability and solubility. Regarding the function, one of the NCR169 oxidized forms could bind to negatively charged bacterial phospholipids. Furthermore, the positively charged lysine-rich region of NCR169 may be responsible for its antimicrobial activity against Escherichia coli and Sinorhizobium meliloti. This active region was disordered even in the phospholipid bound state, suggesting that the disordered conformation of this region is key to its function. Morphological observations suggested the mechanism of action of NCR169 on bacteria. The present study on NCR169 provides new insights into the structure and function of NCR peptides.
format	article
author	Noriyoshi Isozumi Yuya Masubuchi Tomohiro Imamura Masashi Mori Hironori Koga Shinya Ohki
author_facet	Noriyoshi Isozumi Yuya Masubuchi Tomohiro Imamura Masashi Mori Hironori Koga Shinya Ohki
author_sort	Noriyoshi Isozumi
title	Structure and antimicrobial activity of NCR169, a nodule-specific cysteine-rich peptide of Medicago truncatula
title_short	Structure and antimicrobial activity of NCR169, a nodule-specific cysteine-rich peptide of Medicago truncatula
title_full	Structure and antimicrobial activity of NCR169, a nodule-specific cysteine-rich peptide of Medicago truncatula
title_fullStr	Structure and antimicrobial activity of NCR169, a nodule-specific cysteine-rich peptide of Medicago truncatula
title_full_unstemmed	Structure and antimicrobial activity of NCR169, a nodule-specific cysteine-rich peptide of Medicago truncatula
title_sort	structure and antimicrobial activity of ncr169, a nodule-specific cysteine-rich peptide of medicago truncatula
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/219e7e335d924fcd8a489737c3b2bfd9
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Structure and antimicrobial activity of NCR169, a nodule-specific cysteine-rich peptide of Medicago truncatula

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