NagS is a novel GlcNAc-6P dehydratase.

<p><b>(a)</b> Sensitivity of <i>S. coelicolor</i> mutants to GlcNAc. Spores (5 × 10<sup>5</sup> CFU) of <i>S. coelicolor</i> M145 and its mutant derivatives ∆<i>nagB</i>, SMA11, ∆<i>nagB</i>∆<i>nagS</i>, ∆<i...

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Egile nagusia: Chao Li (145513) (author)
Beste egile batzuk: Mia Urem (22683580) (author), Ioli Kotsogianni (9930187) (author), Josephine Lau (20442343) (author), Chao Du (288036) (author), Somayah S. Elsayed (9192571) (author), Nathaniel I. Martin (847378) (author), Iain W. McNae (840777) (author), Patrick Voskamp (2311429) (author), Christoph Mayer (57204) (author), Sébastien Rigali (724082) (author), Navraj Pannu (10163763) (author), Jan Pieter Abrahams (1429531) (author), Lennart Schada von Borzyskowski (22683583) (author), Gilles P. van Wezel (7838948) (author)
Argitaratua: 2025
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_version_ 1849927625803300864
author Chao Li (145513)
author2 Mia Urem (22683580)
Ioli Kotsogianni (9930187)
Josephine Lau (20442343)
Chao Du (288036)
Somayah S. Elsayed (9192571)
Nathaniel I. Martin (847378)
Iain W. McNae (840777)
Patrick Voskamp (2311429)
Christoph Mayer (57204)
Sébastien Rigali (724082)
Navraj Pannu (10163763)
Jan Pieter Abrahams (1429531)
Lennart Schada von Borzyskowski (22683583)
Gilles P. van Wezel (7838948)
author2_role author
author
author
author
author
author
author
author
author
author
author
author
author
author
author_facet Chao Li (145513)
Mia Urem (22683580)
Ioli Kotsogianni (9930187)
Josephine Lau (20442343)
Chao Du (288036)
Somayah S. Elsayed (9192571)
Nathaniel I. Martin (847378)
Iain W. McNae (840777)
Patrick Voskamp (2311429)
Christoph Mayer (57204)
Sébastien Rigali (724082)
Navraj Pannu (10163763)
Jan Pieter Abrahams (1429531)
Lennart Schada von Borzyskowski (22683583)
Gilles P. van Wezel (7838948)
author_role author
dc.creator.none.fl_str_mv Chao Li (145513)
Mia Urem (22683580)
Ioli Kotsogianni (9930187)
Josephine Lau (20442343)
Chao Du (288036)
Somayah S. Elsayed (9192571)
Nathaniel I. Martin (847378)
Iain W. McNae (840777)
Patrick Voskamp (2311429)
Christoph Mayer (57204)
Sébastien Rigali (724082)
Navraj Pannu (10163763)
Jan Pieter Abrahams (1429531)
Lennart Schada von Borzyskowski (22683583)
Gilles P. van Wezel (7838948)
dc.date.none.fl_str_mv 2025-11-25T19:00:32Z
dc.identifier.none.fl_str_mv 10.1371/journal.pbio.3003514.g001
dc.relation.none.fl_str_mv https://figshare.com/articles/figure/NagS_is_a_novel_GlcNAc-6P_dehydratase_/30715199
dc.rights.none.fl_str_mv CC BY 4.0
info:eu-repo/semantics/openAccess
dc.subject.none.fl_str_mv Biochemistry
Microbiology
Ecology
Developmental Biology
Inorganic Chemistry
Biological Sciences not elsewhere classified
controls nutrient signaling
also revealed 6
highlighted key residues
glcnac sensing requires
toxicity pathway dependent
6p deacetylase naga
novel glcnac 6
key role
substrate glcnac
novel enzyme
work uncovers
wall leads
unprecedented reaction
substrate mycelium
structural analogue
streptomycetaceae </
streptomyces </
revolves around
promiscuous activity
nature ’
n </
multicellular lifestyle
metabolic checkpoint
medicine makers
lytic dismantling
landmark event
hyphal cell
highly conserved
growth media
function analysis
clinical antibiotics
central metabolism
catalytic inhibitor
antibiotic production
active site
>- acetylglucosamine
6p dehydratase
dc.title.none.fl_str_mv NagS is a novel GlcNAc-6P dehydratase.
dc.type.none.fl_str_mv Image
Figure
info:eu-repo/semantics/publishedVersion
image
description <p><b>(a)</b> Sensitivity of <i>S. coelicolor</i> mutants to GlcNAc. Spores (5 × 10<sup>5</sup> CFU) of <i>S. coelicolor</i> M145 and its mutant derivatives ∆<i>nagB</i>, SMA11, ∆<i>nagB</i>∆<i>nagS</i>, ∆<i>nagB</i>∆<i>nagS</i><sup>C</sup> (∆<i>nagB</i>∆<i>nagS</i> expressing <i>nagS</i>) and ∆<i>nagB</i>∆<i>nagS</i><sup>E</sup> (∆<i>nagB</i>∆<i>nagS</i> with empty plasmid pSET152) were streaked on MM agar plates with 1% mannitol (Mann) and 1% mannitol plus 10 mM GlcNAc (GlcNAc). Strains were cultured for 72 h at 30 °C. Note that <i>nagB</i> mutants can grow in the presence of 10 mM GlcNAc only when SCO4393 (<i>nagS)</i> has been mutated (suppressor SMA11) or deleted. <b>(b)</b> NagS and its role in GlcNAc sensing. Spores of M145 and ∆<i>nagS</i> were plated on MM and R5 with 0, 0.001, 0.01, 0.1, 1, 5, 10, 20, 50, 100, 150, and 200 mM GlcNAc. Note that <i>nagS</i> mutants hardly respond to GlcNAc. <b>(c)</b> Phylogenetic tree of several different types of sugar isomerase (SIS) domain enzymes in bacteria, including NagS, Glucose-6P isomerase (Pgi), Phosphoheptose isomerase (GmhA), <i>N</i>-acetylmuramic acid-6-phosphate etherase (MurQ), Glutamine-fructose-6-phosphate aminotransferase (GlmS), and putative D-galactosamine-6-phosphate deaminase (Agas). The phylogenetic tree was made by MEGA11 (Neighbour-joining method) and built based on the alignment of the amino acid sequences. <b>(d)</b> ITC analysis of NagS with <i>N</i>-acetyl-6-phosphate amino sugar metabolites, namely GlcNAc-6P, ManNAc-6P, and GalNAc-6P. Both GlcNAc-6P and ManNAc-6P are bound well by NagS, while the enzyme did not bind to GalNAc-6P. (<b>e and f</b>) confirmation of NagS products by LC-MS. Extracted ion chromatograms for GlcNAc-6-P (black trace) and its dehydrated product (pink trace) in the enzymatic reaction mixture of GlcNAc-6-P with either active NagS (e) or heat-inactivated NagS <b>(f)</b>. Peaks relating to the product (<i>m</i>/<i>z</i> = 282.0387) are indicated by red arrows. <b>(g)</b> Kinetics of NagS in the presence of 6-PG (0, 0.33, 1 mM). The <i>V</i><sub>0</sub> data used in d were plotted against the substrate concentration, and each assay was performed in triplicate and expressed as a mean ± standard error. The data underlying this Figure can be found in <a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.3003514#pbio.3003514.s022" target="_blank">S1 Data</a>.</p>
eu_rights_str_mv openAccess
id Manara_0a8669a0f6d3e7da187ff5ff91ecc4f8
identifier_str_mv 10.1371/journal.pbio.3003514.g001
network_acronym_str Manara
network_name_str ManaraRepo
oai_identifier_str oai:figshare.com:article/30715199
publishDate 2025
repository.mail.fl_str_mv
repository.name.fl_str_mv
repository_id_str
rights_invalid_str_mv CC BY 4.0
spelling NagS is a novel GlcNAc-6P dehydratase.Chao Li (145513)Mia Urem (22683580)Ioli Kotsogianni (9930187)Josephine Lau (20442343)Chao Du (288036)Somayah S. Elsayed (9192571)Nathaniel I. Martin (847378)Iain W. McNae (840777)Patrick Voskamp (2311429)Christoph Mayer (57204)Sébastien Rigali (724082)Navraj Pannu (10163763)Jan Pieter Abrahams (1429531)Lennart Schada von Borzyskowski (22683583)Gilles P. van Wezel (7838948)BiochemistryMicrobiologyEcologyDevelopmental BiologyInorganic ChemistryBiological Sciences not elsewhere classifiedcontrols nutrient signalingalso revealed 6highlighted key residuesglcnac sensing requirestoxicity pathway dependent6p deacetylase naganovel glcnac 6key rolesubstrate glcnacnovel enzymework uncoverswall leadsunprecedented reactionsubstrate myceliumstructural analoguestreptomycetaceae </streptomyces </revolves aroundpromiscuous activitynature ’n </multicellular lifestylemetabolic checkpointmedicine makerslytic dismantlinglandmark eventhyphal cellhighly conservedgrowth mediafunction analysisclinical antibioticscentral metabolismcatalytic inhibitorantibiotic productionactive site>- acetylglucosamine6p dehydratase<p><b>(a)</b> Sensitivity of <i>S. coelicolor</i> mutants to GlcNAc. Spores (5 × 10<sup>5</sup> CFU) of <i>S. coelicolor</i> M145 and its mutant derivatives ∆<i>nagB</i>, SMA11, ∆<i>nagB</i>∆<i>nagS</i>, ∆<i>nagB</i>∆<i>nagS</i><sup>C</sup> (∆<i>nagB</i>∆<i>nagS</i> expressing <i>nagS</i>) and ∆<i>nagB</i>∆<i>nagS</i><sup>E</sup> (∆<i>nagB</i>∆<i>nagS</i> with empty plasmid pSET152) were streaked on MM agar plates with 1% mannitol (Mann) and 1% mannitol plus 10 mM GlcNAc (GlcNAc). Strains were cultured for 72 h at 30 °C. Note that <i>nagB</i> mutants can grow in the presence of 10 mM GlcNAc only when SCO4393 (<i>nagS)</i> has been mutated (suppressor SMA11) or deleted. <b>(b)</b> NagS and its role in GlcNAc sensing. Spores of M145 and ∆<i>nagS</i> were plated on MM and R5 with 0, 0.001, 0.01, 0.1, 1, 5, 10, 20, 50, 100, 150, and 200 mM GlcNAc. Note that <i>nagS</i> mutants hardly respond to GlcNAc. <b>(c)</b> Phylogenetic tree of several different types of sugar isomerase (SIS) domain enzymes in bacteria, including NagS, Glucose-6P isomerase (Pgi), Phosphoheptose isomerase (GmhA), <i>N</i>-acetylmuramic acid-6-phosphate etherase (MurQ), Glutamine-fructose-6-phosphate aminotransferase (GlmS), and putative D-galactosamine-6-phosphate deaminase (Agas). The phylogenetic tree was made by MEGA11 (Neighbour-joining method) and built based on the alignment of the amino acid sequences. <b>(d)</b> ITC analysis of NagS with <i>N</i>-acetyl-6-phosphate amino sugar metabolites, namely GlcNAc-6P, ManNAc-6P, and GalNAc-6P. Both GlcNAc-6P and ManNAc-6P are bound well by NagS, while the enzyme did not bind to GalNAc-6P. (<b>e and f</b>) confirmation of NagS products by LC-MS. Extracted ion chromatograms for GlcNAc-6-P (black trace) and its dehydrated product (pink trace) in the enzymatic reaction mixture of GlcNAc-6-P with either active NagS (e) or heat-inactivated NagS <b>(f)</b>. Peaks relating to the product (<i>m</i>/<i>z</i> = 282.0387) are indicated by red arrows. <b>(g)</b> Kinetics of NagS in the presence of 6-PG (0, 0.33, 1 mM). The <i>V</i><sub>0</sub> data used in d were plotted against the substrate concentration, and each assay was performed in triplicate and expressed as a mean ± standard error. The data underlying this Figure can be found in <a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.3003514#pbio.3003514.s022" target="_blank">S1 Data</a>.</p>2025-11-25T19:00:32ZImageFigureinfo:eu-repo/semantics/publishedVersionimage10.1371/journal.pbio.3003514.g001https://figshare.com/articles/figure/NagS_is_a_novel_GlcNAc-6P_dehydratase_/30715199CC BY 4.0info:eu-repo/semantics/openAccessoai:figshare.com:article/307151992025-11-25T19:00:32Z
spellingShingle NagS is a novel GlcNAc-6P dehydratase.
Chao Li (145513)
Biochemistry
Microbiology
Ecology
Developmental Biology
Inorganic Chemistry
Biological Sciences not elsewhere classified
controls nutrient signaling
also revealed 6
highlighted key residues
glcnac sensing requires
toxicity pathway dependent
6p deacetylase naga
novel glcnac 6
key role
substrate glcnac
novel enzyme
work uncovers
wall leads
unprecedented reaction
substrate mycelium
structural analogue
streptomycetaceae </
streptomyces </
revolves around
promiscuous activity
nature ’
n </
multicellular lifestyle
metabolic checkpoint
medicine makers
lytic dismantling
landmark event
hyphal cell
highly conserved
growth media
function analysis
clinical antibiotics
central metabolism
catalytic inhibitor
antibiotic production
active site
>- acetylglucosamine
6p dehydratase
status_str publishedVersion
title NagS is a novel GlcNAc-6P dehydratase.
title_full NagS is a novel GlcNAc-6P dehydratase.
title_fullStr NagS is a novel GlcNAc-6P dehydratase.
title_full_unstemmed NagS is a novel GlcNAc-6P dehydratase.
title_short NagS is a novel GlcNAc-6P dehydratase.
title_sort NagS is a novel GlcNAc-6P dehydratase.
topic Biochemistry
Microbiology
Ecology
Developmental Biology
Inorganic Chemistry
Biological Sciences not elsewhere classified
controls nutrient signaling
also revealed 6
highlighted key residues
glcnac sensing requires
toxicity pathway dependent
6p deacetylase naga
novel glcnac 6
key role
substrate glcnac
novel enzyme
work uncovers
wall leads
unprecedented reaction
substrate mycelium
structural analogue
streptomycetaceae </
streptomyces </
revolves around
promiscuous activity
nature ’
n </
multicellular lifestyle
metabolic checkpoint
medicine makers
lytic dismantling
landmark event
hyphal cell
highly conserved
growth media
function analysis
clinical antibiotics
central metabolism
catalytic inhibitor
antibiotic production
active site
>- acetylglucosamine
6p dehydratase