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PMID: 8248265 Published · ppublish English Comparative Study Journal Article Research Support, U.S. Gov't, Non-P.H.S.

The Arabidopsis endoplasmic reticulum retention receptor functions in yeast.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 90 ·No. 23 ·1993-12-01 ·Pages 11433-7

Lee HI, Gal S, Newman TC, Raikhel NV

Abstract

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.

Related Genes
ERD2
MeSH Terms
Amino Acid Sequence Arabidopsis/physiology Biological Transport Cloning, Molecular DNA, Complementary/genetics Endoplasmic Reticulum/physiology Gene Expression Genes, Plant Genetic Complementation Test Intracellular Membranes/metabolism Membrane Proteins/physiology Molecular Sequence Data RNA, Messenger/genetics Receptors, Peptide Saccharomyces cerevisiae/metabolism Saccharomyces cerevisiae Proteins Sequence Alignment Sequence Homology, Amino Acid
Chemicals
DNA, Complementary ERD2 protein, S cerevisiae KDELR1 protein, human Membrane Proteins RNA, Messenger Receptors, Peptide Saccharomyces cerevisiae Proteins
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Lee H I
Michigan State University-Department of Energy, Plant Research Laboratory, Michigan State University, East Lansing 48824-1312.
Gal S
Newman T C
Raikhel N V
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.90.23.11433
Published
1993-12-01
Pages
11433-7
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC47997
Subset
IM
Databases
GENBANK
L23573
External Links
PubMed source DOI: 10.1073/pnas.90.23.11433 PMC Full Text View journal details
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