Eukaryotic Cell
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Eukaryotic Cell, March 2007, p. 388-397, Vol. 6, No. 3
1535-9778/07/$08.00+0     doi:10.1128/EC.00366-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Endoplasmic Reticulum Retention Signal-Dependent Glycylation of the Hsp70/Grp170-Related Pgp1p in Tetrahymena{triangledown} ,{dagger}

Rong Xie, Kathleen M. Clark, and Martin A. Gorovsky*

Department of Biology, University of Rochester, Rochester, New York 14627

Received 20 November 2006/ Accepted 7 December 2006

Glycylation is an uncommon posttranslational modification. It has been found that tubulin glycylation is essential for cell survival in Tetrahymena. Here we describe PGP1, a Tetrahymena gene encoding an Hsp70 homologue that is a novel glycylated protein. Pgp1p is a conserved glycoprotein that localizes within the lumen of the endoplasmic reticulum (ER). We demonstrate that PGP1 is essential for viability and present evidence that both glycosylation and ER retention are necessary but not sufficient for glycylation.

* Corresponding author. Mailing address: Department of Biology, University of Rochester, 425 Hutchison Hall, Rochester, NY 14627. Phone: (585) 275-6988. Fax: (585) 275-2070. E-mail: goro{at}mail.rochester.edu.

{triangledown} Published ahead of print on 22 December 2006.

{dagger} Supplemental material for this article may be found at http://ec.asm.org/.

Eukaryotic Cell, March 2007, p. 388-397, Vol. 6, No. 3
1535-9778/07/$08.00+0     doi:10.1128/EC.00366-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



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