Rice prolamine protein body biogenesis: a BiP-mediated process

• Published in: Science (American Association for the Advancement of Science) 1993-11, Vol.262 (5136), p.1054-1056
• Main Authors: Li, X, Wu, Y, Zhang, D.Z, Gillikin, J.W, Boston, R.S, Franceschi, V.R, Okita, T.W
• Format: Article
• Language: English
• Subjects: Adenosine Triphosphate - pharmacology; Amino Acid Sequence; Amino acids; Analytical, structural and metabolic biochemistry; Antibodies; Biological and medical sciences; Centrifugation; Corn; Detergents; Endoplasmic Reticulum - metabolism; Fundamental and applied biological sciences. Psychology; GLUTELINAS; GLUTELINE; GRAINE; Messenger RNA; Miscellaneous; Molecular Sequence Data; Molecular Weight; Oryza - metabolism; Oryza - ultrastructure; ORYZA SATIVA; Plant biochemical genetics; Plant cells; Plant Proteins - chemistry; Plant Proteins - metabolism; Polyribosomes; Polyribosomes - metabolism; Prolamins; Protein biosynthesis; Protein Folding; Protein synthesis; PROTEINAS; PROTEINE; Proteins; Protoplasts; Puromycin - pharmacology; Rice; SEMILLA; Synthesis
• ISSN: 0036-8075; 1095-9203
• DOI: 10.1126/science.8235623

Rice prolamines are sequestered within the endoplasmic reticulum (ER) lumen even though they lack a lumenal retention signal. Immunochemical and biochemical data show that BiP, a protein that binds lumenal polypeptides, is localized on the surface of the aggregated prolamine protein bodies (PBs). BiP also forms complexes with nascent chains of prolamines in polyribosomes and with free prolamines with distinct adenosine triphosphate sensitivities. Thus, BiP retains prolamines in the lumen by facilitating their folding and assembly into PBs