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Papers In Press, published online ahead of print June 12, 2003
Biochemistry and Cell Biology, SUNY Stony Brook, Stony Brook, NY 11794
Corresponding Author: wlennarz{at}notes.cc.sunysb.edu
At present, there is very limited knowledge about the structural organization of the yeast oligosaccharyl transferase (OT) complex and the function of each of its 9 subunits. Due to the failure of using the yeast two-hybrid system to reveal interactions between the lumenal domains of these subunits, we utilized a membrane permeable, thio-cleavable cross-linking reagent dithiobis-succinimidylpropionate to study the interactions of various OT subunits biochemically. Four essential gene products, Ost1p, Wbp1p, Swp1p and Stt3p were shown to be cross-linked to each other in a pair-wise fashion. In addition, Ost1p was found to be cross-linked to all other 8 OT subunits individually which leads us to propose that Ost1p may reside in the core of the OT complex and could play an important role in its assembly. Ost4p and Ost5p are found to only interact with specific components of OT complex and may function as an additional anchor for optimal stability in the membrane of Stt3p and Ost1p, respectively. Interestingly, Ost3p and Ost6p subunits exhibited a surprisingly identical pattern of cross-linking to other subunits which is consistent with their proposed redundant function. Based on these findings, we analyzed the distribution of the lysine residues which are likely to be involved in cross-linking of OT subunits, and propose that the OT subunits interact with each other through either their transmembrane domains and/or a region proximal to it, rather than through their lumenal or cytoplasmic domains.
J. Biol. Chem, 10.1074/jbc.M305337200
Submitted on May 21, 2003
Revised on June 12, 2003
Accepted on June 12, 2003
New findings on the interactions among the yeast oligosaccharyl transferase subunits using a chemical cross-linker
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