The Post-Translational Modifications, Localization,and Mode of Attachment of Non-Covalently Bound Glucanosyltransglycosylases of Yeast Cell Wall as aKey to Understanding their Functioningстатья
Статья опубликована в высокорейтинговом журнале
Информация о цитировании статьи получена из
Web of Science,
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 9 декабря 2020 г.
Аннотация:Glucan linked to proteins is a natural mega-glycoconjugate (mGC) playing the central roleas a structural component of a yeast cell wall (CW). Regulation of functioning of non-covalentlybound glucanosyltransglycosylases (ncGTGs) that have to remodel mGC to provide CW extension ispoorly understood. We demonstrate that the main ncGTGs Bgl2 and Scw4 have phosphorylated andglutathionylated residues and are represented in CW as different pools of molecules having variousfirmness of attachment. Identified pools contain Bgl2 molecules with unmodified peptides, but differfrom each other in the presence and combination of modified ones, as well as in the presence orabsence of other CW proteins. Correlation of Bgl2 distribution among pools and its N-glycosylationwas not found. Glutathione affects Bgl2 conformation, probably resulting in the mode of its attachmentand enzymatic activity. Bgl2 from the pool of unmodified and monophosphorylated moleculesdemonstrates the ability to fibrillate after isolation from CW. Revealing of Bgl2 microcompartmentsand their mosaic arrangement summarized with the results obtained give the evidence that thefunctioning of ncGTGs in CW can be controlled by reversible post-translational modifications andfacilitated due to their compact localization. The hypothetical scheme of distribution of Bgl2 insideCW is represented