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Insights into the membrane interacting properties of the C-terminal domain of the monotopic glycosyltransferase DGD2 in A. thaliana
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.ORCID iD: 0000-0003-2965-2873
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
(English)Manuscript (preprint) (Other academic)
National Category
Biophysics
Research subject
Biophysics
Identifiers
URN: urn:nbn:se:su:diva-131248OAI: oai:DiVA.org:su-131248DiVA: diva2:936921
Available from: 2016-06-14 Created: 2016-06-14 Last updated: 2016-06-15Bibliographically approved
In thesis
1. Structure and lipid interactions of membrane-associated glycosyltransferases: Cationic patches and anionic lipids regulate biomembrane binding of both GT-A and GT-B enzymes
Open this publication in new window or tab >>Structure and lipid interactions of membrane-associated glycosyltransferases: Cationic patches and anionic lipids regulate biomembrane binding of both GT-A and GT-B enzymes
2016 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

This thesis concerns work on structure and membrane interactions of enzymes involved in lipid synthesis, biomembrane and cell wall regulation and cell defense processes. These proteins, known as glycosyltransferases (GTs), are involved in the transfer of sugar moieties from nucleotide sugars to lipids or chitin polymers. Glycosyltransferases from three types of organisms have been investigated; one is responsible for vital lipid synthesis in Arabidopsis thaliana (atDGD2) and adjusts the lipid content in biomembranes if the plant experiences stressful growth conditions. This enzyme shares many structural features with another GT found in gram-negative bacteria (WaaG). WaaG is however continuously active and involved in synthesis of the protective lipopolysaccharide layer in the cell walls of Escherichia coli. The third type of enzymes investigated here are chitin synthases (ChS) coupled to filamentous growth in the oomycete Saprolegnia monoica. I have investigated two ChS-derived MIT domains that may be involved in membrane interactions within the endosomal pathway.

From analysis of the three-dimensional structure and the amino-acid sequence, some important regions of these very large proteins were selected for in vitro studies. By the use of an array of biophysical methods (e.g. Nuclear Magnetic Resonance, Fluorescence and Circular Dichroism spectroscopy) and directed sequence analyses it was possible to shed light on some important details regarding the structure and membrane-interacting properties of the GTs. The importance of basic amino-acid residues and hydrophobic anchoring segments, both generally and for the abovementioned proteins specifically, is discussed. Also, the topology and amino-acid sequence of GT-B enzymes of the GT4 family are analyzed with emphasis on their biomembrane association modes. The results presented herein regarding the structural and lipid-interacting properties of GTs aid in the general understanding of glycosyltransferase activity. Since GTs are involved in a high number of biochemical processes in vivo it is of outmost importance to understand the underlying processes responsible for their activity, structure and interaction events. The results are likely to be useful for many applications and future experimental design within life sciences and biomedicine.

Place, publisher, year, edition, pages
Stockholm: Department of Biochemistry and Biophysics, Stockholm University, 2016. 81 p.
Keyword
glycosyltransferase, monotopic membrane proteins, galactolipids, NMR, chitin synthase, DGD2, LPS, WaaG, MIT domain
National Category
Biophysics
Research subject
Biophysics
Identifiers
urn:nbn:se:su:diva-131084 (URN)978-91-7649-435-6 (ISBN)
External cooperation:
Public defence
2016-09-16, Magnélisalen, Kemiska övningslaboratoriet, Svante Arrhenius väg 16 B, Stockholm, 10:00 (English)
Opponent
Supervisors
Note

At the time of the doctoral defense, the following paper was unpublished and had a status as follows: Paper 2: Manuscript.

Available from: 2016-08-24 Created: 2016-06-13 Last updated: 2016-09-01Bibliographically approved

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Szpryngiel, ScarlettMäler, Lena
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