GPI-Modified Proteins Non-covalently Attached to Saccharomyces cerevisiae Yeast Cell Wall

Autor: A A Bykova, Tatyana S. Kalebina, Valentina V. Rekstina, Rustam H. Ziganshin

Publikováno v: Biochemistry (Moscow). 84:1513-1520

Yeast cell wall GPI-anchored proteins lack the lipid part of the anchor and are covalently bound to the high-molecular-weight polysaccharides glucan and/or chitin through the mannose residues. They perform many functions, including participation in t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0eb0e43506548190d0e48f5ccfcdad24
https://doi.org/10.1134/s0006297919120101

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

Autor: Irina B. Kudryashova, Yaroslav V. Tkachev, Alice V. Alessenko, Sergei A. Kuznetsov, Alexei A. Adzhubei, Valentina V. Rekstina, Fanis A Sabirzyanov, Natalia E Snalina, Tatyana A. Sabirzyanova, Rustam H. Ziganshin, Tatyana S. Kalebina, Anastasia A Bykova

Publikováno v: International Journal of Molecular Sciences
Volume 21
Issue 21
International Journal of Molecular Sciences, Vol 21, Iss 8304, p 8304 (2020)

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

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::476a42f146ccc9df411c762587666819
https://pubmed.ncbi.nlm.nih.gov/33167499

Structural model of amyloid fibrils for amyloidogenic peptide from Bgl2p–glucantransferase of S. cerevisiae cell wall and its modifying analog. New morphology of amyloid fibrils

Autor: Elena Yu. Gorbunova, Elizaveta I. Grigorashvili, Anna V. Glyakina, Valentina V. Rekstina, Tatyana S. Kalebina, Nikita V. Dovidchenko, Mariya Yu. Suvorina, Leila G. Mustaeva, Alexey D. Nikulin, Alexey K. Surin, Olga M. Selivanova, Oxana V. Galzitskaya

Publikováno v: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1864:1489-1499

We performed a comparative study of the process of amyloid formation by short homologous peptides with a substitution of aspartate for glutamate in position 2 - VDSWNVLVAG (AspNB) and VESWNVLVAG (GluNB) - with unblocked termini. Peptide AspNB (residu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8e47061e904545919bd3f6326bacb6de
https://doi.org/10.1016/j.bbapap.2016.08.002

C-Terminal sequence is involved in the incorporation of Bgl2p glucanosyltransglycosylase in the cell wall of Saccharomyces cerevisiae

Autor: Alexei A. Adzhubei, Valentina V. Rekstina, F A Sabirzyanov, Tatyana A. Sabirzyanova, Tatyana S. Kalebina

Publikováno v: FEMS Yeast Research. 18

A cell wall (CW) provides a protective barrier for a yeast cell and is a firm structure that nevertheless dynamically changes during cell's growth. Bgl2p is a non-covalently anchored glucanosyltransglycosylase in the CW of the yeast Saccharomyces cer

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::69668c03482ec6186e77b63f0bed061c
https://doi.org/10.1093/femsyr/fox093

Amyloidogenic peptides of yeast cell wall glucantransferase Bgl2p as a model for the investigation of its pH-dependent fibril formation

Autor: Anton A. Gorkovskii, Valentina V. Rekstina, Minna Groenning, Tatyana S. Kalebina, Irina B. Kudryashova, Evgeny E. Bezsonov, Oxana V. Galzitskaya, Gennady V. Semisotnov, I.O. Selyakh, Rustam H. Ziganshin, Igor S. Kulaev, Sergei A. Kuznetsov

Publikováno v: Prion. 7:175-184

The pH-dependence of the ability of Bgl2p to form fibrils was studied using synthetic peptides with potential amyloidogenic determinants (PADs) predicted in the Bgl2p sequence. Three PADs, FTIFVGV, SWNVLVA and NAFS, were selected on the basis of comb

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::96fdccb6178be8fc026c538e79ebeb09
https://doi.org/10.4161/pri.22992