High impact information on SWP1

• The beta and delta subunits of the oligosaccharyltransferase are encoded by the WBP1 and SWP1 genes [1].
• Swp1p is a 30 kDa type I transmembrane protein and essential for cell viability [2].
• We found that Ost2p and Stt3p have only their N terminus located in the cytosol, whereas Ost3p and Swp1p have only their C terminus oriented in the cytosol [3].
• The 60/62 component represents differentially glycosylated forms of a protein that has sequence homology to ribophorin I. Wbp1p and Swp1p reveal homology to mammalian OST 48 and ribophorin II, respectively [4].
• Due to the challenges with purifying the active enzyme complex for detailed biophysical studies, a systematic study to express, isolate, and characterize the soluble domains of three of the largest subunits in the complex (Nlt1p, Wbp1p, and Swp1p) is reported [5].

Biological context of SWP1

• An enzymatically active complex was isolated from microsomal membranes from Saccharomyces cerevisiae, which is composed of four proteins: Wbp1p and Swp1p (previously found to be encoded by two essential genes necessary for N-glycosylation in vivo and in vitro) and two additional proteins with a molecular mass of 60/62 kDa and 34 kDa [4].

Associations of SWP1 with chemical compounds

• The beta and delta subunits were shown to correspond to the 45-kDa Wbp1 glycoprotein and the 30-kDa Swp1 protein, respectively [6].

References