دورية أكاديمية
Structure and functional impact of glycosaminoglycan modification of HSulf-2 endosulfatase revealed by atomic force microscopy and mass spectrometry
| العنوان: | Structure and functional impact of glycosaminoglycan modification of HSulf-2 endosulfatase revealed by atomic force microscopy and mass spectrometry |
|---|---|
| المؤلفون: | Seffouh, Ilham, Bilong, Mélanie, Przybylski, Cédric, El Omrani, Nesrine, Poyer, Salomé, Lamour, Guillaume, Clément, Marie-Jeanne, Boustany, Rebecca-Joe, Gout, Evelyne, Gonnet, Florence, Vivès, Romain, R, Daniel, Régis |
| المساهمون: | Université Paris-Saclay, Institut de biologie structurale (IBS - UMR 5075), Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA), Centre National de la Recherche Scientifique (CNRS), Laboratoire Analyse, Modélisation et Matériaux pour la Biologie et l'Environnement (LAMBE - UMR 8587), Université d'Évry-Val-d'Essonne (UEVE)-Institut de Chimie - CNRS Chimie (INC-CNRS)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-CY Cergy Paris Université (CY) |
| المصدر: | ISSN: 2045-2322. |
| بيانات النشر: | HAL CCSD Nature Publishing Group |
| سنة النشر: | 2023 |
| المجموعة: | Université Paris Seine: ComUE (HAL) |
| مصطلحات موضوعية: | [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], [CHIM.ANAL]Chemical Sciences/Analytical chemistry, [SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biophysics, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM] |
| الوصف: | International audience ; |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| العلاقة: | hal-04348199; https://hal.science/hal-04348199Test; https://hal.science/hal-04348199/documentTest; https://hal.science/hal-04348199/file/Seffouh_et_al-2023-Scientific_Reports.pdfTest |
| DOI: | 10.1038/s41598-023-49147-5 |
| الإتاحة: | https://doi.org/10.1038/s41598-023-49147-5Test https://hal.science/hal-04348199Test https://hal.science/hal-04348199/documentTest https://hal.science/hal-04348199/file/Seffouh_et_al-2023-Scientific_Reports.pdfTest |
| حقوق: | info:eu-repo/semantics/OpenAccess |
| رقم الانضمام: | edsbas.14AC4697 |
| قاعدة البيانات: | BASE |
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Recently, HSulf-2 was shown to exhibit an unusual post-translational modification consisting of a sulfated glycosaminoglycan chain. This study describes the structural characterization of this glycosaminoglycan (GAG) and provides new data on its impact on the catalytic properties of HSulf-2. The unrevealed nature of this GAG chain is identified as a chondroitin/dermatan sulfate (CS/DS) mixed chain, as shown by mass spectrometry combined with NMR analysis. It consists primarily of 6-<jats:italic>O</jats:italic> and 4-<jats:italic>O</jats:italic> monosulfated disaccharide units, with a slight predominance of the 4-<jats:italic>O</jats:italic>-sulfation. Using atomic force microscopy, we show that this unique post-translational modification dramatically impacts the enzyme hydrodynamic volume. We identified human hyaluronidase-4 as a secreted hydrolase that can digest HSulf-2 GAG chain. We also showed that HSulf-2 is able to efficiently 6-<jats:italic>O</jats:italic>-desulfate antithrombin III binding pentasaccharide motif, and that this activity was enhanced upon removal of the GAG chain. Finally, we identified five N-glycosylation sites on the protein and showed that, although required, reduced N-glycosylation profiles were sufficient to sustain HSulf-2 integrity.</jats:p> ) Array ( [Name] => TypeDocument [Label] => Document Type [Group] => TypDoc [Data] => article in journal/newspaper ) Array ( [Name] => Language [Label] => Language [Group] => Lang [Data] => English ) Array ( [Name] => NoteTitleSource [Label] => Relation [Group] => SrcInfo [Data] => hal-04348199; https://hal.science/hal-04348199; https://hal.science/hal-04348199/document; https://hal.science/hal-04348199/file/Seffouh_et_al-2023-Scientific_Reports.pdf ) Array ( [Name] => DOI [Label] => DOI [Group] => ID [Data] => 10.1038/s41598-023-49147-5 ) Array ( [Name] => URL [Label] => Availability [Group] => URL [Data] => https://doi.org/10.1038/s41598-023-49147-5<br />https://hal.science/hal-04348199<br />https://hal.science/hal-04348199/document<br />https://hal.science/hal-04348199/file/Seffouh_et_al-2023-Scientific_Reports.pdf ) Array ( [Name] => Copyright [Label] => Rights [Group] => Cpyrght [Data] => info:eu-repo/semantics/OpenAccess ) Array ( [Name] => AN [Label] => Accession Number [Group] => ID [Data] => edsbas.14AC4697 ) |
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