Soluble proteins retained in the lumen of the endoplasmic reticulum (ER) contain a carboxyl-terminal tetrapeptide sequence that functions presumably to recycle these proteins from a subsequent compartment. Biochemical and genetic evidence indicate that the ERD2 gene product is the receptor for these ER retention signals. Here we report the identification of a cDNA clone from Arabidopsis thaliana (aERD2) similar in sequence and size to members of the ERD2 gene family. Southern and Northern blot analyses indicate that Arabidopsis contains a single aERD2 gene which is expressed at different levels in various plant tissues. A functional assay demonstrates that the Arabidopsis homologue, unlike the mammalian protein, can complement the lethal phenotype of the erd2 deletion mutant of Saccharomyces cerevisiae, indicating that this protein may have a similar function in plants. As the plant protein may have a binding specificity similar to the human Erd2 protein but can function in yeast, we suggest that the plant homologue is the functional link between yeast and animals.
|Original language||English (US)|
|Number of pages||5|
|Journal||Proceedings of the National Academy of Sciences of the United States of America|
|State||Published - Dec 1 1993|
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