Abstract
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.
Publication types
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Research Support, N.I.H., Extramural
MeSH terms
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ATP-Binding Cassette Transporters / biosynthesis
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ATP-Binding Cassette Transporters / metabolism*
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Amino Acid Sequence
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Animals
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Endoplasmic Reticulum / genetics
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Endoplasmic Reticulum / metabolism*
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Glutamine / metabolism
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Glycine / metabolism*
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Glycoproteins / metabolism*
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HSP70 Heat-Shock Proteins / metabolism*
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Protein Processing, Post-Translational
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Protein Sorting Signals / physiology*
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / metabolism
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Sequence Alignment
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Sequence Homology, Amino Acid
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Tetrahymena / genetics*
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Tetrahymena / metabolism*
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Tyrosine / metabolism
Substances
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ATP-Binding Cassette Transporters
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Glycoproteins
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HSP70 Heat-Shock Proteins
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Protein Sorting Signals
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Recombinant Proteins
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glucose-regulated protein 170
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Glutamine
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Tyrosine
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Glycine