{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Rekstina VV"],"funding":["Russian Foundation for Basic Research","Russian Science Foundation"],"pagination":["E8304"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7663962"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["21(21)"],"pubmed_abstract":["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 aff"],"journal":["International journal of molecular sciences"],"pubmed_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."],"pmcid":["PMC7663962"],"funding_grant_id":["grant number 18-14-00321","18-34-00915mol_a, 20-04-01144 A"],"pubmed_authors":["Snalina NE","Kuznetsov SA","Adzhubei AA","Sabirzyanov FA","Kudryashova IB","Kalebina TS","Tkachev YV","Bykova AA","Alessenko AV","Sabirzyanova TA","Rekstina VV","Ziganshin RH"],"additional_accession":[]},"is_claimable":false,"name":"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.","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 aff","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Nov","modification":"2026-05-01T10:09:45.581Z","creation":"2020-11-19T16:59:24Z"},"accession":"S-EPMC7663962","cross_references":{"pubmed":["33167499"],"doi":["10.3390/ijms21218304"]}}