Researcher:
Yunt, Zeynep Sabahat

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Zeynep Sabahat

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Yunt

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Yunt, Zeynep Sabahat

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2020 - 20212

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    Proximal biotinylation-based combinatory approach for isolating integral plasma membrane proteins
    (Amer Chemical Soc, 2020) N/A; Department of Molecular Biology and Genetics; N/A; N/A; N/A; Department of Molecular Biology and Genetics; Akdağ, Mehmet; Yunt, Zeynep Sabahat; Kamacıoğlu, Altuğ; Qureshi, Mohammad Haroon; Akarlar, Büşra; Master Student; Teaching Faculty; Master Student; PhD Student; Other; Faculty Member; Department of Molecular Biology and Genetics; Graduate School of Sciences and Engineering; College of Sciences; Graduate School of Sciences and Engineering; Graduate School of Sciences and Engineering; N/A; College of Sciences; N/A; 116178; N/A; N/A; N/A; 105301
    Comprehensive profiling of the cell-surface proteome has been challenging due to the lack of tools for an effective and reproducible way to isolate plasma membrane proteins from mammalian cells. Here we employ a proximity-dependent biotinylation approach to label and isolate plasma membrane proteins without an extra in vitro labeling step, which we call Plasma Membrane-BiolD. The lipid-modified BirA* enzyme (MyrPalm BirA*) was targeted to the inner leaflet of the plasma membrane, where it effectively biotinylated plasma membrane proteins. Biotinylated proteins were then affinity-purified and analyzed by mass spectrometry. Our analysis demonstrates that combining conventional sucrose density gradient centrifugation and Plasma Membrane-BioID is ideal to overcome the inherent limitations of the identification of integral membrane proteins, and it yields highly pure plasma components for downstream proteomic analysis.
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    PublicationOpen Access
    Enzymatic spiroketal formation via oxidative rearrangement of pentangular polyketides
    (Nature Publishing Group (NPG), 2021) Frensch, Britta; Lechtenberg, Thorsten; Kather, Michel; Betschart, Martin; Kammerer, Bernd; Luedeke, Steffen; Mueller, Michael; Piel, Joern; Teufel, Robin; Department of Molecular Biology and Genetics; Yunt, Zeynep Sabahat; Teaching Faculty; Department of Molecular Biology and Genetics; College of Sciences; 116178
    The structural complexity and bioactivity of natural products often depend on enzymatic redox tailoring steps. This is exemplified by the generation of the bisbenzannulated [5,6]-spiroketal pharmacophore in the bacterial rubromycin family of aromatic polyketides, which exhibit a wide array of bioactivities such as the inhibition of HIV reverse transcriptase or DNA helicase. Here we elucidate the complex flavoenzyme-driven formation of the rubromycin pharmacophore that is markedly distinct from conventional (bio)synthetic strategies for spiroketal formation. Accordingly, a polycyclic aromatic precursor undergoes extensive enzymatic oxidative rearrangement catalyzed by two flavoprotein monooxygenases and a flavoprotein oxidase that ultimately results in a drastic distortion of the carbon skeleton. The one-pot in vitro reconstitution of the key enzymatic steps as well as the comprehensive characterization of reactive intermediates allow to unravel the intricate underlying reactions, during which four carbon-carbon bonds are broken and two CO2 become eliminated. This work provides detailed insight into perplexing redox tailoring enzymology that sets the stage for the (chemo)enzymatic production and bioengineering of bioactive spiroketal-containing polyketides.Rubromycin family of natural products belongs to aromatic polyketides with diverse bioactivities, but details of their biosynthesis are limited. Here, the authors report the complete in vitro reconstitution of enzymatic formation of the spiroketal moiety of rubromycin polyketides, driven by flavin-dependent enzymes, and characterize reaction intermediates.