Mayor, S. ; Menon, A. K. ; Cross, G. A. (1991) Transfer of glycosyl-phosphatidylinositol membrane anchors to polypeptide acceptors in a cell-free system Journal of Cell Biology, 114 (1). pp. 61-71. ISSN 0021-9525
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Official URL: http://jcb.rupress.org/content/114/1/61.abstract
Related URL: http://dx.doi.org/10.1083/jcb.114.1.61
Abstract
Glycosylinositol phospholipid (GPI) membrane anchors are the sole means of membrane attachment of a large number of cell surface proteins, including the variant surface glycoproteins (VSGs) of the parasitic protozoan, Trypanosoma brucei. Biosynthetic data suggest that GPI-anchored proteins are synthesized with carboxy-terminal extensions that are immediately replaced by GPI, suggesting the existence of preformed GPI species available for transfer to the nascent protein in the ER. Candidate precursor glycolipids having a linear sequence indistinguishable from the conserved core structure found on all GPI anchors, have been characterized in T. brucei. In this paper we describe the transfer of three GPI variants to endogenous VSG in vitro. GPI addition is not reduced by inhibitors of protein synthesis and does not require ATP or GTP, consistent with a transpeptidation mechanism.
Item Type: | Article |
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Source: | Copyright of this article belongs to Rockefeller University Press. |
ID Code: | 26713 |
Deposited On: | 08 Dec 2010 13:20 |
Last Modified: | 17 May 2016 10:00 |
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