Yil102c-A is a Functional Homologue of the DPMII Subunit of Dolichyl Phosphate Mannose Synthase in <i>Saccharomyces cerevisiae</i>
In a wide range of organisms, dolichyl phosphate mannose (DPM) synthase is a complex of tree proteins Dpm1, Dpm2, and Dpm3. However, in the yeast <i>Saccharomyces cerevisiae</i>, it is believed to be a single Dpm1 protein. The function of Dpm3 is performed in <i>S. cerevisiae</i...
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MDPI AG
2020-11-01
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| Series: | International Journal of Molecular Sciences |
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| author | Sebastian Piłsyk Urszula Perlinska-Lenart Anna Janik Elżbieta Gryz Marta Ajchler-Adamska Joanna S. Kruszewska |
| author_facet | Sebastian Piłsyk Urszula Perlinska-Lenart Anna Janik Elżbieta Gryz Marta Ajchler-Adamska Joanna S. Kruszewska |
| author_sort | Sebastian Piłsyk |
| collection | DOAJ |
| description | In a wide range of organisms, dolichyl phosphate mannose (DPM) synthase is a complex of tree proteins Dpm1, Dpm2, and Dpm3. However, in the yeast <i>Saccharomyces cerevisiae</i>, it is believed to be a single Dpm1 protein. The function of Dpm3 is performed in <i>S. cerevisiae</i> by the C-terminal transmembrane domain of the catalytic subunit Dpm1. Until present, the regulatory Dpm2 protein has not been found in <i>S. cerevisiae</i>. In this study, we show that, in fact, the Yil102c-A protein interacts directly with Dpm1 in <i>S. cerevisiae</i> and influences its DPM synthase activity. Deletion of the <i>YIL102c-A</i> gene is lethal, and this phenotype is reversed by the <i>dpm2</i> gene from <i>Trichoderma reesei</i>. Functional analysis of Yil102c-A revealed that it also interacts with glucosylphosphatidylinositol-<i>N</i>-acetylglucosaminyl transferase (GPI-GnT), similar to DPM2 in human cells. Taken together, these results show that Yil102c-A is a functional homolog of DPMII from <i>T. reesei</i> and DPM2 from humans. |
| first_indexed | 2024-03-10T14:34:50Z |
| format | Article |
| id | doaj.art-4f87301f2d22462aa53ccdbb9d5caefb |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-10T14:34:50Z |
| publishDate | 2020-11-01 |
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| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-4f87301f2d22462aa53ccdbb9d5caefb2023-11-20T22:16:00ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672020-11-012123893810.3390/ijms21238938Yil102c-A is a Functional Homologue of the DPMII Subunit of Dolichyl Phosphate Mannose Synthase in <i>Saccharomyces cerevisiae</i>Sebastian Piłsyk0Urszula Perlinska-Lenart1Anna Janik2Elżbieta Gryz3Marta Ajchler-Adamska4Joanna S. Kruszewska5Institute of Biochemistry and Biophysics Polish Academy of Sciences, 02-106 Warsaw, PolandInstitute of Biochemistry and Biophysics Polish Academy of Sciences, 02-106 Warsaw, PolandInstitute of Biochemistry and Biophysics Polish Academy of Sciences, 02-106 Warsaw, PolandInstitute of Biochemistry and Biophysics Polish Academy of Sciences, 02-106 Warsaw, PolandInstitute of Biochemistry and Biophysics Polish Academy of Sciences, 02-106 Warsaw, PolandInstitute of Biochemistry and Biophysics Polish Academy of Sciences, 02-106 Warsaw, PolandIn a wide range of organisms, dolichyl phosphate mannose (DPM) synthase is a complex of tree proteins Dpm1, Dpm2, and Dpm3. However, in the yeast <i>Saccharomyces cerevisiae</i>, it is believed to be a single Dpm1 protein. The function of Dpm3 is performed in <i>S. cerevisiae</i> by the C-terminal transmembrane domain of the catalytic subunit Dpm1. Until present, the regulatory Dpm2 protein has not been found in <i>S. cerevisiae</i>. In this study, we show that, in fact, the Yil102c-A protein interacts directly with Dpm1 in <i>S. cerevisiae</i> and influences its DPM synthase activity. Deletion of the <i>YIL102c-A</i> gene is lethal, and this phenotype is reversed by the <i>dpm2</i> gene from <i>Trichoderma reesei</i>. Functional analysis of Yil102c-A revealed that it also interacts with glucosylphosphatidylinositol-<i>N</i>-acetylglucosaminyl transferase (GPI-GnT), similar to DPM2 in human cells. Taken together, these results show that Yil102c-A is a functional homolog of DPMII from <i>T. reesei</i> and DPM2 from humans.https://www.mdpi.com/1422-0067/21/23/8938<i>Trichoderma reesei</i>DPM2GPI-GnT |
| spellingShingle | Sebastian Piłsyk Urszula Perlinska-Lenart Anna Janik Elżbieta Gryz Marta Ajchler-Adamska Joanna S. Kruszewska Yil102c-A is a Functional Homologue of the DPMII Subunit of Dolichyl Phosphate Mannose Synthase in <i>Saccharomyces cerevisiae</i> International Journal of Molecular Sciences <i>Trichoderma reesei</i> DPM2 GPI-GnT |
| title | Yil102c-A is a Functional Homologue of the DPMII Subunit of Dolichyl Phosphate Mannose Synthase in <i>Saccharomyces cerevisiae</i> |
| title_full | Yil102c-A is a Functional Homologue of the DPMII Subunit of Dolichyl Phosphate Mannose Synthase in <i>Saccharomyces cerevisiae</i> |
| title_fullStr | Yil102c-A is a Functional Homologue of the DPMII Subunit of Dolichyl Phosphate Mannose Synthase in <i>Saccharomyces cerevisiae</i> |
| title_full_unstemmed | Yil102c-A is a Functional Homologue of the DPMII Subunit of Dolichyl Phosphate Mannose Synthase in <i>Saccharomyces cerevisiae</i> |
| title_short | Yil102c-A is a Functional Homologue of the DPMII Subunit of Dolichyl Phosphate Mannose Synthase in <i>Saccharomyces cerevisiae</i> |
| title_sort | yil102c a is a functional homologue of the dpmii subunit of dolichyl phosphate mannose synthase in i saccharomyces cerevisiae i |
| topic | <i>Trichoderma reesei</i> DPM2 GPI-GnT |
| url | https://www.mdpi.com/1422-0067/21/23/8938 |
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