Rice prolamine protein body biogenesis: a BiP-mediated process.
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.
Li
X
X
Department of Genetics and Cell Biology, Washington State University, Pullman 99164.
Wu
Y
Y
Zhang
D Z
DZ
Gillikin
J W
JW
Boston
R S
RS
Franceschi
V R
VR
Okita
T W
TW
D000255:Adenosine Triphosphate / Q000494:pharmacology; D000595:Amino Acid Sequence; D004721:Endoplasmic Reticulum / Q000378:metabolism; D008969:Molecular Sequence Data; D008970:Molecular Weight; D012275:Oryza / Q000378:metabolism* / Q000648:ultrastructure; D010940:Plant Proteins / Q000737:chemistry / Q000378:metabolism*; D011132:Polyribosomes / Q000378:metabolism; D055315:Prolamins; D017510:Protein Folding; D011691:Puromycin / Q000494:pharmacology
D010940:Plant Proteins; D055315:Prolamins; D011691:Puromycin; D000255:Adenosine Triphosphate