A conserved rhizobial peptidase that interacts with host-derived symbiotic peptides

Abstract In the Medicago truncatula-Sinorhizobium meliloti symbiosis, chemical signaling initiates rhizobial infection of root nodule tissue, where a large portion of the bacteria are endocytosed into root nodule cells to function in nitrogen-fixing organelles. These intracellular bacteria are subje...

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Autores principales:	Alex B. Benedict, Prithwi Ghosh, Samuel M. Scott, Joel S. Griffitts
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/f25b87e33a2248518a6263b8b323cd77
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spelling	oai:doaj.org-article:f25b87e33a2248518a6263b8b323cd772021-12-02T15:02:23ZA conserved rhizobial peptidase that interacts with host-derived symbiotic peptides10.1038/s41598-021-91394-x2045-2322https://doaj.org/article/f25b87e33a2248518a6263b8b323cd772021-06-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-91394-xhttps://doaj.org/toc/2045-2322Abstract In the Medicago truncatula-Sinorhizobium meliloti symbiosis, chemical signaling initiates rhizobial infection of root nodule tissue, where a large portion of the bacteria are endocytosed into root nodule cells to function in nitrogen-fixing organelles. These intracellular bacteria are subjected to an arsenal of plant-derived nodule-specific cysteine-rich (NCR) peptides, which induce the physiological changes that accompany nitrogen fixation. NCR peptides drive these intracellular bacteria toward terminal differentiation. The bacterial peptidase HrrP was previously shown to degrade host-derived NCR peptides and give the bacterial symbionts greater fitness at the expense of host fitness. The hrrP gene is found in roughly 10% of Sinorhizobium isolates, as it is carried on an accessory plasmid. The objective of the present study is to identify peptidase genes in the core genome of S. meliloti that modulate symbiotic outcome in a manner similar to the accessory hrrP gene. In an overexpression screen of annotated peptidase genes, we identified one such symbiosis-associated peptidase (sap) gene, sapA (SMc00451). When overexpressed, sapA leads to a significant decrease in plant fitness. Its promoter is active in root nodules, with only weak expression evident under free-living conditions. The SapA enzyme can degrade a broad range of NCR peptides in vitro.Alex B. BenedictPrithwi GhoshSamuel M. ScottJoel S. GriffittsNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-10 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Alex B. Benedict Prithwi Ghosh Samuel M. Scott Joel S. Griffitts A conserved rhizobial peptidase that interacts with host-derived symbiotic peptides
description	Abstract In the Medicago truncatula-Sinorhizobium meliloti symbiosis, chemical signaling initiates rhizobial infection of root nodule tissue, where a large portion of the bacteria are endocytosed into root nodule cells to function in nitrogen-fixing organelles. These intracellular bacteria are subjected to an arsenal of plant-derived nodule-specific cysteine-rich (NCR) peptides, which induce the physiological changes that accompany nitrogen fixation. NCR peptides drive these intracellular bacteria toward terminal differentiation. The bacterial peptidase HrrP was previously shown to degrade host-derived NCR peptides and give the bacterial symbionts greater fitness at the expense of host fitness. The hrrP gene is found in roughly 10% of Sinorhizobium isolates, as it is carried on an accessory plasmid. The objective of the present study is to identify peptidase genes in the core genome of S. meliloti that modulate symbiotic outcome in a manner similar to the accessory hrrP gene. In an overexpression screen of annotated peptidase genes, we identified one such symbiosis-associated peptidase (sap) gene, sapA (SMc00451). When overexpressed, sapA leads to a significant decrease in plant fitness. Its promoter is active in root nodules, with only weak expression evident under free-living conditions. The SapA enzyme can degrade a broad range of NCR peptides in vitro.
format	article
author	Alex B. Benedict Prithwi Ghosh Samuel M. Scott Joel S. Griffitts
author_facet	Alex B. Benedict Prithwi Ghosh Samuel M. Scott Joel S. Griffitts
author_sort	Alex B. Benedict
title	A conserved rhizobial peptidase that interacts with host-derived symbiotic peptides
title_short	A conserved rhizobial peptidase that interacts with host-derived symbiotic peptides
title_full	A conserved rhizobial peptidase that interacts with host-derived symbiotic peptides
title_fullStr	A conserved rhizobial peptidase that interacts with host-derived symbiotic peptides
title_full_unstemmed	A conserved rhizobial peptidase that interacts with host-derived symbiotic peptides
title_sort	conserved rhizobial peptidase that interacts with host-derived symbiotic peptides
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/f25b87e33a2248518a6263b8b323cd77
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A conserved rhizobial peptidase that interacts with host-derived symbiotic peptides

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