期刊
BIOCHEMISTRY AND BIOPHYSICS REPORTS
卷 18, 期 -, 页码 -出版社
ELSEVIER
DOI: 10.1016/j.bbrep.2019.01.010
关键词
HSulf-2; 6-O-Endosulfatase; Sulfatase; Heparan sulfate; Formylglycine; Mass spectrometry
资金
- CNRS [GDR 3739]
- GDR GAG [GDR 3739]
- French Infrastructure for Integrated Structural Biology (FRISBI) [ANR-10-INSB-05-01]
- Investissements d'avenir program Glyco@Alps [ANR-15-IDEX-02]
- Agence Nationale de la Recherche [ANR-12-BSV8-0023, ANR-17-CE11-0040]
- Universite Grenoble Alpes (UGA AGIR program)
- Agence Nationale de la Recherche (ANR) [ANR-17-CE11-0040] Funding Source: Agence Nationale de la Recherche (ANR)
The human 6-O-endosulfatases HSulf-1 and -2 catalyze the region-selective hydrolysis of the 6-O-sulfate group of the glucosamine residues within sulfated domains of heparan sulfate, thereby ensuring a unique and original post-biosynthetic modification of the cell surface proteoglycans. While numerous studies point out the role of HSulf-2 in crucial physiological processes as well as in pathological conditions particularly in cancer, its structural organization in two chains and its functional properties remain poorly understood. In this study, we report the first characterization by mass spectrometry (MS) of HSulf-2. An average molecular weight of 133,115 Da was determined for the whole enzyme by MALDI-TOF MS, i.e. higher than the naked amino acid backbone (98,170 Da), highlighting a significant contribution of post-translational modifications. The HSulf-2 protein sequence was determined by Nano-LC-MS/MS, leading to 63% coverage and indicating at least four N-glycosylation sites at Asn 108, 147, 174 and 217. These results provide a platform for further structural investigations of the HSulf enzymes, aiming at deciphering the role of each chain in the substrate binding and specificities and in the catalytic activities.
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