The predominance of nucleotidyl activation in bacterial phosphonate biosynthesis
Phosphonate modifications can be present on microbial cell surfaces. Here the authors perform bioinformatics analyses and observe a widespread occurrence of nucleotidyltransferase-encoding genes in bacterial phosphonate biosynthesis and functionally characterize two of the identified phosphonate spe...
Main Authors: | , , , , , , , , , , , , , , |
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Format: | Article |
Language: | English |
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Nature Portfolio
2019-08-01
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Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-019-11627-6 |
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author | Kyle Rice Kissa Batul Jacqueline Whiteside Jayne Kelso Monica Papinski Edward Schmidt Alena Pratasouskaya Dacheng Wang Rebecca Sullivan Christopher Bartlett Joel T. Weadge Marc W. Van der Kamp Gabriel Moreno-Hagelsieb Michael D. Suits Geoff P. Horsman |
author_facet | Kyle Rice Kissa Batul Jacqueline Whiteside Jayne Kelso Monica Papinski Edward Schmidt Alena Pratasouskaya Dacheng Wang Rebecca Sullivan Christopher Bartlett Joel T. Weadge Marc W. Van der Kamp Gabriel Moreno-Hagelsieb Michael D. Suits Geoff P. Horsman |
author_sort | Kyle Rice |
collection | DOAJ |
description | Phosphonate modifications can be present on microbial cell surfaces. Here the authors perform bioinformatics analyses and observe a widespread occurrence of nucleotidyltransferase-encoding genes in bacterial phosphonate biosynthesis and functionally characterize two of the identified phosphonate specific cytidylyltransferases (PntCs) and determine the crystal structure of T. denticola PntC. |
first_indexed | 2024-12-14T14:39:29Z |
format | Article |
id | doaj.art-851a3355841b4f708a43a502942c9977 |
institution | Directory Open Access Journal |
issn | 2041-1723 |
language | English |
last_indexed | 2024-12-14T14:39:29Z |
publishDate | 2019-08-01 |
publisher | Nature Portfolio |
record_format | Article |
series | Nature Communications |
spelling | doaj.art-851a3355841b4f708a43a502942c99772022-12-21T22:57:27ZengNature PortfolioNature Communications2041-17232019-08-0110111210.1038/s41467-019-11627-6The predominance of nucleotidyl activation in bacterial phosphonate biosynthesisKyle Rice0Kissa Batul1Jacqueline Whiteside2Jayne Kelso3Monica Papinski4Edward Schmidt5Alena Pratasouskaya6Dacheng Wang7Rebecca Sullivan8Christopher Bartlett9Joel T. Weadge10Marc W. Van der Kamp11Gabriel Moreno-Hagelsieb12Michael D. Suits13Geoff P. Horsman14Department of Chemistry & Biochemistry, Wilfrid Laurier UniversityDepartment of Chemistry & Biochemistry, Wilfrid Laurier UniversityDepartment of Chemistry & Biochemistry, Wilfrid Laurier UniversityDepartment of Chemistry & Biochemistry, Wilfrid Laurier UniversityDepartment of Chemistry & Biochemistry, Wilfrid Laurier UniversityDepartment of Chemistry & Biochemistry, Wilfrid Laurier UniversityDepartment of Chemistry & Biochemistry, Wilfrid Laurier UniversityDepartment of Chemistry & Biochemistry, Wilfrid Laurier UniversityDepartment of Chemistry & Biochemistry, Wilfrid Laurier UniversityDepartment of Biology, Wilfrid Laurier UniversityDepartment of Biology, Wilfrid Laurier UniversitySchool of Biochemistry, University of BristolDepartment of Biology, Wilfrid Laurier UniversityDepartment of Chemistry & Biochemistry, Wilfrid Laurier UniversityDepartment of Chemistry & Biochemistry, Wilfrid Laurier UniversityPhosphonate modifications can be present on microbial cell surfaces. Here the authors perform bioinformatics analyses and observe a widespread occurrence of nucleotidyltransferase-encoding genes in bacterial phosphonate biosynthesis and functionally characterize two of the identified phosphonate specific cytidylyltransferases (PntCs) and determine the crystal structure of T. denticola PntC.https://doi.org/10.1038/s41467-019-11627-6 |
spellingShingle | Kyle Rice Kissa Batul Jacqueline Whiteside Jayne Kelso Monica Papinski Edward Schmidt Alena Pratasouskaya Dacheng Wang Rebecca Sullivan Christopher Bartlett Joel T. Weadge Marc W. Van der Kamp Gabriel Moreno-Hagelsieb Michael D. Suits Geoff P. Horsman The predominance of nucleotidyl activation in bacterial phosphonate biosynthesis Nature Communications |
title | The predominance of nucleotidyl activation in bacterial phosphonate biosynthesis |
title_full | The predominance of nucleotidyl activation in bacterial phosphonate biosynthesis |
title_fullStr | The predominance of nucleotidyl activation in bacterial phosphonate biosynthesis |
title_full_unstemmed | The predominance of nucleotidyl activation in bacterial phosphonate biosynthesis |
title_short | The predominance of nucleotidyl activation in bacterial phosphonate biosynthesis |
title_sort | predominance of nucleotidyl activation in bacterial phosphonate biosynthesis |
url | https://doi.org/10.1038/s41467-019-11627-6 |
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