The Post-Translational Modifications, Localization, and Mode of Attachment of Non-Covalently Bound Glucanosyltransglycosylases of Yeast Cell Wall as a Key to Understanding their Functioning
Glucan linked to proteins is a natural mega-glycoconjugate (mGC) playing the central role as a structural component of a yeast cell wall (CW). Regulation of functioning of non-covalently bound glucanosyltransglycosylases (ncGTGs) that have to remodel mGC to provide CW extension is poorly understood....
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| Format: | Article |
| Language: | English |
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2020-11-01
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| Series: | International Journal of Molecular Sciences |
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| author | Valentina V. Rekstina Tatyana A. Sabirzyanova Fanis A. Sabirzyanov Alexei A. Adzhubei Yaroslav V. Tkachev Irina B. Kudryashova Natalia E. Snalina Anastasia A. Bykova Alice V. Alessenko Rustam H. Ziganshin Sergei A. Kuznetsov Tatyana S. Kalebina |
| author_facet | Valentina V. Rekstina Tatyana A. Sabirzyanova Fanis A. Sabirzyanov Alexei A. Adzhubei Yaroslav V. Tkachev Irina B. Kudryashova Natalia E. Snalina Anastasia A. Bykova Alice V. Alessenko Rustam H. Ziganshin Sergei A. Kuznetsov Tatyana S. Kalebina |
| author_sort | Valentina V. Rekstina |
| collection | DOAJ |
| description | Glucan linked to proteins is a natural mega-glycoconjugate (mGC) playing the central role as a structural component of a yeast cell wall (CW). Regulation of functioning of non-covalently bound glucanosyltransglycosylases (ncGTGs) that have to remodel mGC to provide CW extension is poorly understood. We demonstrate that the main ncGTGs Bgl2 and Scw4 have phosphorylated and glutathionylated residues and are represented in CW as different pools of molecules having various firmness of attachment. Identified pools contain Bgl2 molecules with unmodified peptides, but differ from each other in the presence and combination of modified ones, as well as in the presence or absence of other CW proteins. Correlation of Bgl2 distribution among pools and its N-glycosylation was not found. Glutathione affects Bgl2 conformation, probably resulting in the mode of its attachment and enzymatic activity. Bgl2 from the pool of unmodified and monophosphorylated molecules demonstrates the ability to fibrillate after isolation from CW. Revealing of Bgl2 microcompartments and their mosaic arrangement summarized with the results obtained give the evidence that the functioning of ncGTGs in CW can be controlled by reversible post-translational modifications and facilitated due to their compact localization. The hypothetical scheme of distribution of Bgl2 inside CW is represented. |
| first_indexed | 2024-03-10T15:04:19Z |
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| id | doaj.art-a4b6fd4f6e334d70b849468c60355c0c |
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| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-10T15:04:19Z |
| publishDate | 2020-11-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-a4b6fd4f6e334d70b849468c60355c0c2023-11-20T19:54:27ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672020-11-012121830410.3390/ijms21218304The Post-Translational Modifications, Localization, and Mode of Attachment of Non-Covalently Bound Glucanosyltransglycosylases of Yeast Cell Wall as a Key to Understanding their FunctioningValentina V. Rekstina0Tatyana A. Sabirzyanova1Fanis A. Sabirzyanov2Alexei A. Adzhubei3Yaroslav V. Tkachev4Irina B. Kudryashova5Natalia E. Snalina6Anastasia A. Bykova7Alice V. Alessenko8Rustam H. Ziganshin9Sergei A. Kuznetsov10Tatyana S. Kalebina11Department of Molecular Biology, Faculty of Biology, Lomonosov Moscow State University, Moscow 119991, RussiaDepartment of Molecular Biology, Faculty of Biology, Lomonosov Moscow State University, Moscow 119991, RussiaDepartment of Molecular Biology, Faculty of Biology, Lomonosov Moscow State University, Moscow 119991, RussiaEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow 119991, RussiaEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow 119991, RussiaDepartment of Molecular Biology, Faculty of Biology, Lomonosov Moscow State University, Moscow 119991, RussiaEmanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow 119334, RussiaDepartment of Molecular Biology, Faculty of Biology, Lomonosov Moscow State University, Moscow 119991, RussiaEmanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow 119334, RussiaShemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, RussiaInstitute of Biological Sciences, University of Rostock, 18059 Rostock, GermanyDepartment of Molecular Biology, Faculty of Biology, Lomonosov Moscow State University, Moscow 119991, RussiaGlucan linked to proteins is a natural mega-glycoconjugate (mGC) playing the central role as a structural component of a yeast cell wall (CW). Regulation of functioning of non-covalently bound glucanosyltransglycosylases (ncGTGs) that have to remodel mGC to provide CW extension is poorly understood. We demonstrate that the main ncGTGs Bgl2 and Scw4 have phosphorylated and glutathionylated residues and are represented in CW as different pools of molecules having various firmness of attachment. Identified pools contain Bgl2 molecules with unmodified peptides, but differ from each other in the presence and combination of modified ones, as well as in the presence or absence of other CW proteins. Correlation of Bgl2 distribution among pools and its N-glycosylation was not found. Glutathione affects Bgl2 conformation, probably resulting in the mode of its attachment and enzymatic activity. Bgl2 from the pool of unmodified and monophosphorylated molecules demonstrates the ability to fibrillate after isolation from CW. Revealing of Bgl2 microcompartments and their mosaic arrangement summarized with the results obtained give the evidence that the functioning of ncGTGs in CW can be controlled by reversible post-translational modifications and facilitated due to their compact localization. The hypothetical scheme of distribution of Bgl2 inside CW is represented.https://www.mdpi.com/1422-0067/21/21/8304cell wallglucanosyltransglycosylasespost-translational modificationsmicrocompartmentsBgl2Scw4 |
| spellingShingle | Valentina V. Rekstina Tatyana A. Sabirzyanova Fanis A. Sabirzyanov Alexei A. Adzhubei Yaroslav V. Tkachev Irina B. Kudryashova Natalia E. Snalina Anastasia A. Bykova Alice V. Alessenko Rustam H. Ziganshin Sergei A. Kuznetsov Tatyana S. Kalebina The Post-Translational Modifications, Localization, and Mode of Attachment of Non-Covalently Bound Glucanosyltransglycosylases of Yeast Cell Wall as a Key to Understanding their Functioning International Journal of Molecular Sciences cell wall glucanosyltransglycosylases post-translational modifications microcompartments Bgl2 Scw4 |
| title | The Post-Translational Modifications, Localization, and Mode of Attachment of Non-Covalently Bound Glucanosyltransglycosylases of Yeast Cell Wall as a Key to Understanding their Functioning |
| title_full | The Post-Translational Modifications, Localization, and Mode of Attachment of Non-Covalently Bound Glucanosyltransglycosylases of Yeast Cell Wall as a Key to Understanding their Functioning |
| title_fullStr | The Post-Translational Modifications, Localization, and Mode of Attachment of Non-Covalently Bound Glucanosyltransglycosylases of Yeast Cell Wall as a Key to Understanding their Functioning |
| title_full_unstemmed | The Post-Translational Modifications, Localization, and Mode of Attachment of Non-Covalently Bound Glucanosyltransglycosylases of Yeast Cell Wall as a Key to Understanding their Functioning |
| title_short | The Post-Translational Modifications, Localization, and Mode of Attachment of Non-Covalently Bound Glucanosyltransglycosylases of Yeast Cell Wall as a Key to Understanding their Functioning |
| title_sort | post translational modifications localization and mode of attachment of non covalently bound glucanosyltransglycosylases of yeast cell wall as a key to understanding their functioning |
| topic | cell wall glucanosyltransglycosylases post-translational modifications microcompartments Bgl2 Scw4 |
| url | https://www.mdpi.com/1422-0067/21/21/8304 |
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