Essential role for diacylglycerol in protein transport from the yeast Golgi complex
Article Abstract:
Defects in Sac1p, an integral membrane protein connected with inositol-5-phosphates, can lead to changes in phospholipid metabolism, thus increasing the pool of diacylglycerol (DAG) in the Golgi. This in turn reduces the need for Sec14p, the yeast phosphatidylinositol transfer protein which is required for the production of secretory vesicles from the Golgi. It is possible that the key role of Sec14p is to ensure a sufficient pool of DAG in the Golgi. This assists in the production of secretory vesicles. There are clear links between Sec14p pathway activity and the relationship between Sac1p and inositol phospholipid metabolism.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1997
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Template-imprinted nanostructured surfaces for protein recognition
Article Abstract:
Radio-frequency glow-discharge plasma deposition has been used to create polymeric thin films around proteins coated with disaccharide molecules. It was possible to covalently incorporate the coated sugars into the plasma film while causing minimal damage to the underlying protein. Competitive adsorption of a binary protein mixture showed a highly preferential adsorption of a template protein, BSA, onto its own imprint. Protein recognition is evident only in competitive adsorption, indicating that exchange is taking place between nonspecifically adsorbed non-template protein and the solution-phase template protein.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1999
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Crystal structure of the Saccharomyces cerevisiae phosphatidylinositol-transfer protein
Article Abstract:
The yeast phosphatidylinositol-transfer protein (Sec14) is made up of 12 alpha-helices, six beta-strands, eight 3(sub10)-helices and has two clear domains. Two bound molecules of beta-OG were identified in the Sec14 electronic density map, and the detergent acyl chains extend away from the Sec14 interior. In contrast, the headgroups are oriented inwards. This research gives the first structural information about the function of a phosphatidylinositol-transfer protein.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1998
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