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Property-controlling Enzymes at the Membrane Interface

Ge, Changrong, 1980- (author)
Stockholms universitet,Institutionen för biokemi och biofysik,Åke Wieslander
Wieslander, Åke, Professor (thesis advisor)
Stockholms universitet,Institutionen för biokemi och biofysik
Guerin, Marcelo E., Ikerbasque Research Professor (opponent)
University of the Basque Country
 (creator_code:org_t)
ISBN 9789174473308
Stockholm : Department of Biochemistry and Biophysics, Stockholm University, 2011
English 80 s.
  • Doctoral thesis (other academic/artistic)
Abstract Subject headings
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  • Monotopic proteins represent a specialized group of membrane proteins in that they are engaged in biochemical events taking place at the membrane interface. In particular, the monotopic lipid-synthesizing enzymes are able to synthesize amphiphilic lipid products by catalyzing two biochemically distinct molecules (substrates) at the membrane interface. Thus, from an evolutionary point of view, anchoring into the membrane interface enables monotopic enzymes to confer sensitivity to a changing environment by regulating their activities in the lipid biosynthetic pathways in order to maintain a certain membrane homeostasis. We are focused on a plant lipid-synthesizing enzyme DGD2 involved in phosphate shortage stress, and analyzed the potentially important lipid anchoring segments of it, by a set of biochemical and biophysical approaches. A mechanism was proposed to explain how DGD2 adjusts its activity to maintain a proper membrane. In addition, a multivariate-based bioinformatics approach was used to predict the lipid-binding segments for GT-B fold monotopic enzymes. In contrast, a soluble protein Myr1 from yeast, implicated in vesicular traffic, was also proposed to be a membrane stress sensor as it is able to exert different binding properties to stressed membranes, which is probably due to the presence of strongly plus-charged clusters in the protein. Moreover, a bacterial monotopic enzyme MGS was found to be able to induce massive amounts of intracellular vesicles in Escherichia coli cells. The mechanisms involve several steps: binding, bilayer lateral expansion, stimulation of lipid synthesis, and membrane bending. Proteolytic and mutant studies indicate that plus-charged residues and the scaffold-like structure of MGS are crucial for the vesiculation process. Hence, a number of features are involved governing the behaviour of monotopic membrane proteins at the lipid bilayer interface.

Subject headings

NATURVETENSKAP  -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
NATURAL SCIENCES  -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)

Keyword

monotopic membrane protein
lipid-protein interaction
membrane curvature
glycosyltransferase
Rossmann fold
Biochemistry
Biokemi
biokemi
Biochemistry

Publication and Content Type

vet (subject category)
dok (subject category)

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