Activity test of NagS homologs in vitro and in vivo.

Activity test of NagS homologs in vitro and in vivo.

<p><b>(a)</b> Comparison of amino acid sequences of <i>S. coelicolor</i> NagS and its homologs. These are homologs from <i>Streptacidiphilus jiangxiensis</i> (TrEMBL A0A1H7F721), <i>Clostridium amylolyticum</i> (TrEMBL A0A1M6IM34), <i>Paeni...

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Bibliografiska uppgifter
Huvudupphovsman: Chao Li (145513) (author)
Övriga upphovsmän: 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)
Publicerad: 2025
Ämnen:
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 ’
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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
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Sammanfattning:<p><b>(a)</b> Comparison of amino acid sequences of <i>S. coelicolor</i> NagS and its homologs. These are homologs from <i>Streptacidiphilus jiangxiensis</i> (TrEMBL A0A1H7F721), <i>Clostridium amylolyticum</i> (TrEMBL A0A1M6IM34), <i>Paenibacillus selenitireducens</i> (TrEMBL A0A1T2XKX6), and <i>Acidothermus cellulolyticus</i> (TrEMBL A0LSD9). The amino acid identities with <i>S. coelicolor</i> NagS are 65.5%, 33.2%, 25.7%, and 35.7%, respectively. Absorbance changes detected at 230 nm when incubating 2 mM GlcNAc-6P with proteins from <i>S. jiangxiensis</i> <b>(b)</b>, <i>C. amylolyticum</i> <b>(c)</b>, <i>P. selenitireducens</i> <b>(d),</b> and <i>A. cellulolyticus</i> <b>(e)</b> at 30 °C. Increased absorbance means that GlcNAc-6P was dehydrated by the incubated NagS homologs. This shows that only the protein from <i>S. jiangxiensis</i> is a true NagS homolog. <b>(f)</b> In vivo activity test of NagS homologs. GlcNAc sensitivity of ∆<i>nagB</i>∆<i>nagS</i> harboring clones expressing the homologs from <i>S. jiangxiensis</i> (A0A1H7F721), <i>C. amylolyticum</i> (A0A1M6IM34), <i>P. selenitireducens</i> (A0A1T2XKX6), and <i>A. cellulolyticus</i> (A0LSD9) were grown on MM agar supplemented with 1% mannitol (Mann) and 1% mannitol plus 10 mM GlcNAc (GlcNAc). As expected based on the enzymatic activities, only the complementation of A0A1H7F721 restored GlcNAc sensitivity. This supports the phylogenetic analysis that true NagS orthologs are only found in <i>Streptomycetaceae</i>. 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> <p>(TIF)</p>

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