The Phosphohistidine Phosphatase SixA Targets a Phosphotransferase System

ABSTRACT SixA, a well-conserved protein found in proteobacteria, actinobacteria, and cyanobacteria, is the only reported example of a bacterial phosphohistidine phosphatase. A single protein target of SixA has been reported to date: the Escherichia coli histidine kinase ArcB. The present work analyz...

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Autores principales:	Jane E. Schulte, Mark Goulian
Formato:	article
Lenguaje:	EN
Publicado:	American Society for Microbiology 2018
Materias:	CvrA histidine phosphatase histidine phosphorylation PtsN YcgO Microbiology QR1-502
Acceso en línea:	https://doaj.org/article/9d89cf3a2d8c4d378a00cab6aeba222c
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spelling	oai:doaj.org-article:9d89cf3a2d8c4d378a00cab6aeba222c2021-11-15T15:52:18ZThe Phosphohistidine Phosphatase SixA Targets a Phosphotransferase System10.1128/mBio.01666-182150-7511https://doaj.org/article/9d89cf3a2d8c4d378a00cab6aeba222c2018-12-01T00:00:00Zhttps://journals.asm.org/doi/10.1128/mBio.01666-18https://doaj.org/toc/2150-7511ABSTRACT SixA, a well-conserved protein found in proteobacteria, actinobacteria, and cyanobacteria, is the only reported example of a bacterial phosphohistidine phosphatase. A single protein target of SixA has been reported to date: the Escherichia coli histidine kinase ArcB. The present work analyzes an ArcB-independent growth defect of a sixA deletion in E. coli. A screen for suppressors, analysis of various mutants, and phosphorylation assays indicate that SixA modulates phosphorylation of the nitrogen-related phosphotransferase system (PTSNtr). The PTSNtr is a widely conserved bacterial pathway that regulates diverse metabolic processes through the phosphorylation states of its protein components, EINtr, NPr, and EIIANtr, which receive phosphoryl groups on histidine residues. However, a mechanism for dephosphorylating this system has not been reported. The results presented here suggest a model in which SixA removes phosphoryl groups from the PTSNtr by acting on NPr. This work uncovers a new role for the phosphohistidine phosphatase SixA and, through factors that affect SixA expression or activity, may point to additional inputs that regulate the PTSNtr. IMPORTANCE One common means to regulate protein activity is through phosphorylation. Protein phosphatases exist to reverse this process, returning the protein to the unphosphorylated form. The vast majority of protein phosphatases that have been identified target phosphoserine, phosphotheronine, and phosphotyrosine. A widely conserved phosphohistidine phosphatase was identified in Escherichia coli 20 years ago but remains relatively understudied. The present work shows that this phosphatase modulates the nitrogen-related phosphotransferase system, a pathway that is regulated by nitrogen and carbon metabolism and affects diverse aspects of bacterial physiology. Until now, there was no known mechanism for removing phosphoryl groups from this pathway.Jane E. SchulteMark GoulianAmerican Society for MicrobiologyarticleCvrAhistidine phosphatasehistidine phosphorylationPtsNYcgOMicrobiologyQR1-502ENmBio, Vol 9, Iss 6 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	CvrA histidine phosphatase histidine phosphorylation PtsN YcgO Microbiology QR1-502
spellingShingle	CvrA histidine phosphatase histidine phosphorylation PtsN YcgO Microbiology QR1-502 Jane E. Schulte Mark Goulian The Phosphohistidine Phosphatase SixA Targets a Phosphotransferase System
description	ABSTRACT SixA, a well-conserved protein found in proteobacteria, actinobacteria, and cyanobacteria, is the only reported example of a bacterial phosphohistidine phosphatase. A single protein target of SixA has been reported to date: the Escherichia coli histidine kinase ArcB. The present work analyzes an ArcB-independent growth defect of a sixA deletion in E. coli. A screen for suppressors, analysis of various mutants, and phosphorylation assays indicate that SixA modulates phosphorylation of the nitrogen-related phosphotransferase system (PTSNtr). The PTSNtr is a widely conserved bacterial pathway that regulates diverse metabolic processes through the phosphorylation states of its protein components, EINtr, NPr, and EIIANtr, which receive phosphoryl groups on histidine residues. However, a mechanism for dephosphorylating this system has not been reported. The results presented here suggest a model in which SixA removes phosphoryl groups from the PTSNtr by acting on NPr. This work uncovers a new role for the phosphohistidine phosphatase SixA and, through factors that affect SixA expression or activity, may point to additional inputs that regulate the PTSNtr. IMPORTANCE One common means to regulate protein activity is through phosphorylation. Protein phosphatases exist to reverse this process, returning the protein to the unphosphorylated form. The vast majority of protein phosphatases that have been identified target phosphoserine, phosphotheronine, and phosphotyrosine. A widely conserved phosphohistidine phosphatase was identified in Escherichia coli 20 years ago but remains relatively understudied. The present work shows that this phosphatase modulates the nitrogen-related phosphotransferase system, a pathway that is regulated by nitrogen and carbon metabolism and affects diverse aspects of bacterial physiology. Until now, there was no known mechanism for removing phosphoryl groups from this pathway.
format	article
author	Jane E. Schulte Mark Goulian
author_facet	Jane E. Schulte Mark Goulian
author_sort	Jane E. Schulte
title	The Phosphohistidine Phosphatase SixA Targets a Phosphotransferase System
title_short	The Phosphohistidine Phosphatase SixA Targets a Phosphotransferase System
title_full	The Phosphohistidine Phosphatase SixA Targets a Phosphotransferase System
title_fullStr	The Phosphohistidine Phosphatase SixA Targets a Phosphotransferase System
title_full_unstemmed	The Phosphohistidine Phosphatase SixA Targets a Phosphotransferase System
title_sort	phosphohistidine phosphatase sixa targets a phosphotransferase system
publisher	American Society for Microbiology
publishDate	2018
url	https://doaj.org/article/9d89cf3a2d8c4d378a00cab6aeba222c
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The Phosphohistidine Phosphatase SixA Targets a Phosphotransferase System

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