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Biosynthesis of the thiazole moiety of thiamin in Escherichia coli : Identification of an acyldisulfide-linked protein–protein conjugate that is functionally...
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| Zeitschriftentitel: | Proceedings of the National Academy of Sciences |
|---|---|
| Personen und Körperschaften: | , , , , |
| In: | Proceedings of the National Academy of Sciences, 98, 2001, 15, S. 8513-8518 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Proceedings of the National Academy of Sciences
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| Schlagwörter: |
| author_facet |
Xi, Jun Ge, Ying Kinsland, Cynthia McLafferty, Fred W. Begley, Tadhg P. Xi, Jun Ge, Ying Kinsland, Cynthia McLafferty, Fred W. Begley, Tadhg P. |
|---|---|
| author |
Xi, Jun Ge, Ying Kinsland, Cynthia McLafferty, Fred W. Begley, Tadhg P. |
| spellingShingle |
Xi, Jun Ge, Ying Kinsland, Cynthia McLafferty, Fred W. Begley, Tadhg P. Proceedings of the National Academy of Sciences Biosynthesis of the thiazole moiety of thiamin in Escherichia coli : Identification of an acyldisulfide-linked protein–protein conjugate that is functionally analogous to the ubiquitin/E1 complex Multidisciplinary |
| author_sort |
xi, jun |
| spelling |
Xi, Jun Ge, Ying Kinsland, Cynthia McLafferty, Fred W. Begley, Tadhg P. 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.141226698 <jats:p> A covalently linked protein–protein conjugate between ThiF and ThiS thiocarboxylate was found in a partially purified coexpressed ThiF/ThiS protein mixture by using Fourier transform mass spectrometry. The Cys-184 of ThiF and the C terminus of ThiS thiocarboxylate were identified to be involved in the formation of this complex by using both mutagenesis and chemical modification methods. A complementation study of <jats:italic> Escherichia coli thiF <jats:sup>−</jats:sup> </jats:italic> using <jats:italic>thiF</jats:italic> (C184S) suggests that this conjugate is an essential intermediate involved in the biosynthesis of the thiazole moiety of thiamin. This ThiF/ThiS conjugate is the first characterized example of a unique acyldisulfide intermediate in a biosynthetic system. This protein conjugate is also an example of an ubiquitin-E1 like protein–protein conjugate in prokaryotes and supports a strong evolutionary link between thiamin biosynthesis and the ubiquitin conjugating system. </jats:p> Biosynthesis of the thiazole moiety of thiamin in <i>Escherichia coli</i> : Identification of an acyldisulfide-linked protein–protein conjugate that is functionally analogous to the ubiquitin/E1 complex Proceedings of the National Academy of Sciences |
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Proceedings of the National Academy of Sciences, 2001 |
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Proceedings of the National Academy of Sciences, 2001 |
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| title |
Biosynthesis of the thiazole moiety of thiamin in Escherichia coli : Identification of an acyldisulfide-linked protein–protein conjugate that is functionally analogous to the ubiquitin/E1 complex |
| title_unstemmed |
Biosynthesis of the thiazole moiety of thiamin in Escherichia coli : Identification of an acyldisulfide-linked protein–protein conjugate that is functionally analogous to the ubiquitin/E1 complex |
| title_full |
Biosynthesis of the thiazole moiety of thiamin in Escherichia coli : Identification of an acyldisulfide-linked protein–protein conjugate that is functionally analogous to the ubiquitin/E1 complex |
| title_fullStr |
Biosynthesis of the thiazole moiety of thiamin in Escherichia coli : Identification of an acyldisulfide-linked protein–protein conjugate that is functionally analogous to the ubiquitin/E1 complex |
| title_full_unstemmed |
Biosynthesis of the thiazole moiety of thiamin in Escherichia coli : Identification of an acyldisulfide-linked protein–protein conjugate that is functionally analogous to the ubiquitin/E1 complex |
| title_short |
Biosynthesis of the thiazole moiety of thiamin in Escherichia coli : Identification of an acyldisulfide-linked protein–protein conjugate that is functionally analogous to the ubiquitin/E1 complex |
| title_sort |
biosynthesis of the thiazole moiety of thiamin in
<i>escherichia coli</i>
: identification of an acyldisulfide-linked protein–protein conjugate that is functionally analogous to the ubiquitin/e1 complex |
| topic |
Multidisciplinary |
| url |
http://dx.doi.org/10.1073/pnas.141226698 |
| publishDate |
2001 |
| physical |
8513-8518 |
| description |
<jats:p>
A covalently linked protein–protein conjugate between ThiF and ThiS thiocarboxylate was found in a partially purified coexpressed ThiF/ThiS protein mixture by using Fourier transform mass spectrometry. The Cys-184 of ThiF and the C terminus of ThiS thiocarboxylate were identified to be involved in the formation of this complex by using both mutagenesis and chemical modification methods. A complementation study of
<jats:italic>
Escherichia coli thiF
<jats:sup>−</jats:sup>
</jats:italic>
using
<jats:italic>thiF</jats:italic>
(C184S) suggests that this conjugate is an essential intermediate involved in the biosynthesis of the thiazole moiety of thiamin. This ThiF/ThiS conjugate is the first characterized example of a unique acyldisulfide intermediate in a biosynthetic system. This protein conjugate is also an example of an ubiquitin-E1 like protein–protein conjugate in prokaryotes and supports a strong evolutionary link between thiamin biosynthesis and the ubiquitin conjugating system.
</jats:p> |
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| author | Xi, Jun, Ge, Ying, Kinsland, Cynthia, McLafferty, Fred W., Begley, Tadhg P. |
| author_facet | Xi, Jun, Ge, Ying, Kinsland, Cynthia, McLafferty, Fred W., Begley, Tadhg P., Xi, Jun, Ge, Ying, Kinsland, Cynthia, McLafferty, Fred W., Begley, Tadhg P. |
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| description | <jats:p> A covalently linked protein–protein conjugate between ThiF and ThiS thiocarboxylate was found in a partially purified coexpressed ThiF/ThiS protein mixture by using Fourier transform mass spectrometry. The Cys-184 of ThiF and the C terminus of ThiS thiocarboxylate were identified to be involved in the formation of this complex by using both mutagenesis and chemical modification methods. A complementation study of <jats:italic> Escherichia coli thiF <jats:sup>−</jats:sup> </jats:italic> using <jats:italic>thiF</jats:italic> (C184S) suggests that this conjugate is an essential intermediate involved in the biosynthesis of the thiazole moiety of thiamin. This ThiF/ThiS conjugate is the first characterized example of a unique acyldisulfide intermediate in a biosynthetic system. This protein conjugate is also an example of an ubiquitin-E1 like protein–protein conjugate in prokaryotes and supports a strong evolutionary link between thiamin biosynthesis and the ubiquitin conjugating system. </jats:p> |
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| imprint_str_mv | Proceedings of the National Academy of Sciences, 2001 |
| institution | DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229 |
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| physical | 8513-8518 |
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| series | Proceedings of the National Academy of Sciences |
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| spelling | Xi, Jun Ge, Ying Kinsland, Cynthia McLafferty, Fred W. Begley, Tadhg P. 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.141226698 <jats:p> A covalently linked protein–protein conjugate between ThiF and ThiS thiocarboxylate was found in a partially purified coexpressed ThiF/ThiS protein mixture by using Fourier transform mass spectrometry. The Cys-184 of ThiF and the C terminus of ThiS thiocarboxylate were identified to be involved in the formation of this complex by using both mutagenesis and chemical modification methods. A complementation study of <jats:italic> Escherichia coli thiF <jats:sup>−</jats:sup> </jats:italic> using <jats:italic>thiF</jats:italic> (C184S) suggests that this conjugate is an essential intermediate involved in the biosynthesis of the thiazole moiety of thiamin. This ThiF/ThiS conjugate is the first characterized example of a unique acyldisulfide intermediate in a biosynthetic system. This protein conjugate is also an example of an ubiquitin-E1 like protein–protein conjugate in prokaryotes and supports a strong evolutionary link between thiamin biosynthesis and the ubiquitin conjugating system. </jats:p> Biosynthesis of the thiazole moiety of thiamin in <i>Escherichia coli</i> : Identification of an acyldisulfide-linked protein–protein conjugate that is functionally analogous to the ubiquitin/E1 complex Proceedings of the National Academy of Sciences |
| spellingShingle | Xi, Jun, Ge, Ying, Kinsland, Cynthia, McLafferty, Fred W., Begley, Tadhg P., Proceedings of the National Academy of Sciences, Biosynthesis of the thiazole moiety of thiamin in Escherichia coli : Identification of an acyldisulfide-linked protein–protein conjugate that is functionally analogous to the ubiquitin/E1 complex, Multidisciplinary |
| title | Biosynthesis of the thiazole moiety of thiamin in Escherichia coli : Identification of an acyldisulfide-linked protein–protein conjugate that is functionally analogous to the ubiquitin/E1 complex |
| title_full | Biosynthesis of the thiazole moiety of thiamin in Escherichia coli : Identification of an acyldisulfide-linked protein–protein conjugate that is functionally analogous to the ubiquitin/E1 complex |
| title_fullStr | Biosynthesis of the thiazole moiety of thiamin in Escherichia coli : Identification of an acyldisulfide-linked protein–protein conjugate that is functionally analogous to the ubiquitin/E1 complex |
| title_full_unstemmed | Biosynthesis of the thiazole moiety of thiamin in Escherichia coli : Identification of an acyldisulfide-linked protein–protein conjugate that is functionally analogous to the ubiquitin/E1 complex |
| title_short | Biosynthesis of the thiazole moiety of thiamin in Escherichia coli : Identification of an acyldisulfide-linked protein–protein conjugate that is functionally analogous to the ubiquitin/E1 complex |
| title_sort | biosynthesis of the thiazole moiety of thiamin in <i>escherichia coli</i> : identification of an acyldisulfide-linked protein–protein conjugate that is functionally analogous to the ubiquitin/e1 complex |
| title_unstemmed | Biosynthesis of the thiazole moiety of thiamin in Escherichia coli : Identification of an acyldisulfide-linked protein–protein conjugate that is functionally analogous to the ubiquitin/E1 complex |
| topic | Multidisciplinary |
| url | http://dx.doi.org/10.1073/pnas.141226698 |