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PMID: 8235623 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

Rice prolamine protein body biogenesis: a BiP-mediated process.

Science (New York, N.Y.) ·Vol. 262 ·No. 5136 ·1993-11-12 ·Pages 1054-6

Li X, Wu Y, Zhang DZ, Gillikin JW, Boston RS, Franceschi VR, Okita TW

Abstract

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.

MeSH Terms
Adenosine Triphosphate/pharmacology Amino Acid Sequence Endoplasmic Reticulum/metabolism Molecular Sequence Data Molecular Weight Oryza/metabolism,ultrastructure Plant Proteins/chemistry,metabolism Polyribosomes/metabolism Prolamins Protein Folding Puromycin/pharmacology
Chemicals
Plant Proteins Prolamins Puromycin Adenosine Triphosphate
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Li X
Department of Genetics and Cell Biology, Washington State University, Pullman 99164.
Wu Y
Zhang D Z
Gillikin J W
Boston R S
Franceschi V R
Okita T W
Article Info
Journal
Science (New York, N.Y.)
Abbr.
Science
ISSN
0036-8075
Published
1993-11-12
Pages
1054-6
Language
English
Region
United States
NLM ID
0404511
Subset
IM
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