title: The tobacco homolog of mammalian calreticulin is present in protein complexes in vivo.
abstract: The analysis of protein sorting signals responsible for the retention of reticuloplasmins (RPLs), a group of soluble proteins that reside in the lumen of the endoplasmic reticulum (ER), has revealed a structural similarity between mammalian and plant ER retention signals. We present evidence that the corresponding epitope is conserved in a vast family of soluble ER resident proteins. Microsequences of RPL60 and RPL90, two abundant members of this family, show high sequence similarity with mammalian calreticulin and endoplasmin. RPL60/calreticulin cofractionates and costains with the lumenal binding protein (BiP). Both proteins were detected in the nuclear envelope and the ER, and in mitotic cells in association with the spindle apparatus and the phragmoplast. Immunoprecipitation of proteins from in vivo-labeled cells demonstrated that RPL60/calreticulin is associated with other polypeptides in a stress- and ATP-dependent fashion. RPL60/calreticulin transcript levels increased rapidly in abundance during the proliferation of the secretory apparatus and the onset of hydrolase secretion in gibberellic acid-treated barley aleurone cells. This induction profile is identical to that of the well-characterized ER chaperones BiP and endoplasmin. However, expression patterns in response to different stress conditions as well as tissue-specific expression patterns indicate that these genes are differentially regulated and may not act in concert.
authors.affiliation: Department of Molecular Genetics, Swedish University of Agricultural Sciences.
authors.forename: J
authors.initials: J
authors.lastname: Denecke
authors.forename: L E
authors.initials: LE
authors.lastname: Carlsson
authors.forename: S
authors.initials: S
authors.lastname: Vidal
authors.forename: A S
authors.initials: AS
authors.lastname: Höglund
authors.forename: B
authors.initials: B
authors.lastname: Ek
authors.forename: M J
authors.initials: MJ
authors.lastname: van Zeijl
authors.forename: K M
authors.initials: KM
authors.lastname: Sinjorgo
authors.forename: E T
authors.initials: ET
authors.lastname: Palva
mesh_terms: D000595:Amino Acid Sequence; D029681:Arabidopsis Proteins; D001483:Base Sequence; D002135:Calcium-Binding Proteins / Q000737:chemistry / Q000235:genetics*; D037282:Calreticulin; D002352:Carrier Proteins / Q000737:chemistry / Q000235:genetics*; D004721:Endoplasmic Reticulum / Q000737:chemistry; D018506:Gene Expression Regulation, Plant; D017343:Genes, Plant; D006360:Heat-Shock Proteins / Q000737:chemistry; D007535:Isomerases / Q000737:chemistry; D018832:Molecular Chaperones / Q000235:genetics; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry / Q000235:genetics*; D010947:Plants, Toxic; D019704:Protein Disulfide-Isomerases; D012261:Ribonucleoproteins / Q000737:chemistry / Q000235:genetics*; D017386:Sequence Homology, Amino Acid; D014026:Nicotiana / Q000737:chemistry / Q000235:genetics*
chemical_list: D029681:Arabidopsis Proteins; D002135:Calcium-Binding Proteins; D037282:Calreticulin; D002352:Carrier Proteins; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D010940:Plant Proteins; D012261:Ribonucleoproteins; C077221:BIP protein, Arabidopsis; D007535:Isomerases; D019704:Protein Disulfide-Isomerases