title: Identification of two novel endoplasmic reticulum body-specific integral membrane proteins.
abstract: The endoplasmic reticulum (ER) body, a large compartment specific to the Brassicales, accumulates β-glucosidase and possibly plays a role in the defense against pathogens and herbivores. Although the ER body is a subdomain of the ER, it is unclear whether any ER body-specific membrane protein exists. In this study, we identified two integral membrane proteins of the ER body in Arabidopsis (Arabidopsis thaliana) and termed them MEMBRANE PROTEIN OF ENDOPLASMIC RETICULUM BODY1 (MEB1) and MEB2. In Arabidopsis, a basic helix-loop-helix transcription factor, NAI1, and an ER body component, NAI2, regulate ER body formation. The expression profiles of MEB1 and MEB2 are similar to those of NAI1, NAI2, and ER body β-glucosidase PYK10 in Arabidopsis. The expression of MEB1 and MEB2 was reduced in the nai1 mutant, indicating that NAI1 regulates the expression of MEB1 and MEB2 genes. MEB1 and MEB2 proteins localize to the ER body membrane but not to the ER network, suggesting that these proteins are specifically recruited to the ER body membrane. MEB1 and MEB2 physically interacted with ER body component NAI2, and they were diffused throughout the ER network in the nai2 mutant, which has no ER body. Heterologous expression of MEB1 and MEB2 in yeast (Saccharomyces cerevisiae) suppresses iron and manganese toxicity, suggesting that MEB1 and MEB2 are metal transporters. These results indicate that the membrane of ER bodies has specific membrane proteins and suggest that the ER body is involved in defense against metal stress as well as pathogens and herbivores.
authors.affiliation: Department of Cell Biology, National Institute for Basic Biology, Okazaki 444-8585, Aichi, Japan.
authors.forename: Kenji
authors.initials: K
authors.lastname: Yamada
authors.forename: Atsushi J
authors.initials: AJ
authors.lastname: Nagano
authors.forename: Momoko
authors.initials: M
authors.lastname: Nishina
authors.forename: Ikuko
authors.initials: I
authors.lastname: Hara-Nishimura
authors.forename: Mikio
authors.initials: M
authors.lastname: Nishimura
mesh_terms: D016960:Agrobacterium tumefaciens / Q000235:genetics / Q000378:metabolism; D000528:Alternaria / Q000472:pathogenicity; D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000235:genetics / Q000378:metabolism* / Q000382:microbiology; D029681:Arabidopsis Proteins / Q000235:genetics / Q000378:metabolism*; D027682:Cation Transport Proteins / Q000235:genetics / Q000378:metabolism; D003470:Culture Media / Q000378:metabolism; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D005670:Fusarium / Q000472:pathogenicity; D018506:Gene Expression Regulation, Plant; D017343:Genes, Plant; D047468:Immunoprecipitation; D007425:Intracellular Membranes / Q000378:metabolism; D007501:Iron / Q000378:metabolism; D008345:Manganese / Q000378:metabolism; D008565:Membrane Proteins / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D008969:Molecular Sequence Data; D010935:Plant Diseases / Q000382:microbiology; D030821:Plants, Genetically Modified / Q000235:genetics / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism
chemical_list: D029681:Arabidopsis Proteins; D027682:Cation Transport Proteins; D003470:Culture Media; D008565:Membrane Proteins; C539717:NAI2 protein, Arabidopsis; D008345:Manganese; D007501:Iron