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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2025
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| _version_ | 1849927625862021120 |
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| 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 | 2025-11-25T19:00:14Z |
| dc.identifier.none.fl_str_mv | 10.1371/journal.pbio.3003514.s009 |
| dc.relation.none.fl_str_mv | https://figshare.com/articles/figure/Activity_test_of_NagS_homologs_in_vitro_and_in_vivo_/30715156 |
| 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 | Activity test of NagS homologs in vitro and in vivo. |
| dc.type.none.fl_str_mv | Image Figure info:eu-repo/semantics/publishedVersion image |
| description | <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> |
| eu_rights_str_mv | openAccess |
| id | Manara_7bb58f19191f9cf0d0d8132db2dc758f |
| identifier_str_mv | 10.1371/journal.pbio.3003514.s009 |
| network_acronym_str | Manara |
| network_name_str | ManaraRepo |
| oai_identifier_str | oai:figshare.com:article/30715156 |
| publishDate | 2025 |
| repository.mail.fl_str_mv | |
| repository.name.fl_str_mv | |
| repository_id_str | |
| rights_invalid_str_mv | CC BY 4.0 |
| spelling | Activity test of NagS homologs in vitro and in vivo.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> 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>2025-11-25T19:00:14ZImageFigureinfo:eu-repo/semantics/publishedVersionimage10.1371/journal.pbio.3003514.s009https://figshare.com/articles/figure/Activity_test_of_NagS_homologs_in_vitro_and_in_vivo_/30715156CC BY 4.0info:eu-repo/semantics/openAccessoai:figshare.com:article/307151562025-11-25T19:00:14Z |
| spellingShingle | Activity test of NagS homologs in vitro and in vivo. 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 | Activity test of NagS homologs in vitro and in vivo. |
| title_full | Activity test of NagS homologs in vitro and in vivo. |
| title_fullStr | Activity test of NagS homologs in vitro and in vivo. |
| title_full_unstemmed | Activity test of NagS homologs in vitro and in vivo. |
| title_short | Activity test of NagS homologs in vitro and in vivo. |
| title_sort | Activity test of NagS homologs in vitro and in vivo. |
| 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 |