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Science 5 August 1988:
Vol. 241. no. 4866, pp. 697 - 699
DOI: 10.1126/science.3399901
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Articles
Science, Vol 241, Issue 4866, 697-699
Copyright © 1988 by American Association for the Advancement of Science
Conversion of a PI-anchored protein to an integral membrane protein by a single amino acid mutation
GL Waneck,
ME Stein,
and
RA Flavell
Biogen Research Corporation, Cambridge, MA 02142.
Qa-2, a cell-surface glycoprotein anchored by phosphatidylinositol (PI), is structurally related to the class I transplantation antigens H-2 K, D, and L, which are integral membrane glycoproteins. The predicted transmembrane segment of Qa-2 differs from those of H-2 K, D, and L by the presence of an aspartate in place of a valine at position 295. A single base change that replaced this aspartate with valine resulted in cell-surface Qa-2 molecules that were insensitive to hydrolysis by a PI-specific phospholipase C and more resistant to papain cleavage, properties shared by H-2D. Cells expressing Asp----Val mutant Qa-2 proteins were still able to attach a PI anchor to endogenous proteins such as Thy-1 and J11D. It therefore appears that this single amino acid change converts Qa-2 from a PI-linked form into an integral membrane protein.
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