Document Detail


Analysis of zeins' ER retention in Xenopus oocytes.
MedLine Citation:
PMID:  8574920     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Zeins, maize storage proteins, are retained in the endoplasmic reticulum (ER) during the intracellular protein targeting process. Hydrophobic interaction has been postulated as the driving force of zeins' aggregation and retention in the ER. Recently, a class of zein (the 27K zein) has been proposed to facilitate zeins' ER retention by anchoring to the ER membrane. This study investigated the significance of the two proposed mechanisms toward zeins' ER retention using Xenopus oocyte. Following injection of the total or 27K zein mRNA, zein's movement within the ER was analyzed based upon the extent of diffusion to the non-injected oocyte half. This study indicates that the total zeins freely move within the lumen of the ER, thus, suggesting that the intermolecular aggregation, leading to insolubility and exclusion from the ER lumenal fluid, may not be essential for zeins' ER retention. This study also suggests that the 27K zein may not facilitate zeins' ER retention by virtue of an anchor to the ER membrane based on its free movement in the ER. Free movement of the total and 27K zeins, under conditions where zein aggregates should form, necessitates a reevaluation of the mechanisms responsible for zein polypeptides' ER retention and protein body formation.
Authors:
D H Lee; O Y Kwon; K Pedersen
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology     Volume:  111     ISSN:  1096-4959     ISO Abbreviation:  Comp. Biochem. Physiol. B, Biochem. Mol. Biol.     Publication Date:  1995 Aug 
Date Detail:
Created Date:  1996-03-14     Completed Date:  1996-03-14     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  9516061     Medline TA:  Comp Biochem Physiol B Biochem Mol Biol     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  533-43     Citation Subset:  IM    
Affiliation:
Department of Biology, Virginia Polytechnic Institute, Blacksburg 24061-0406, USA.
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MeSH Terms
Descriptor/Qualifier:
Animals
Biological Transport
Cell Membrane / metabolism
Endoplasmic Reticulum / chemistry,  metabolism*
Female
Injections
Leucine / metabolism,  pharmacology
Oocytes / drug effects,  physiology*
Protein Biosynthesis
RNA, Messenger / chemistry,  genetics
Time Factors
Tritium
Xenopus laevis
Zein / chemistry,  genetics,  metabolism*
Chemical
Reg. No./Substance:
0/RNA, Messenger; 10028-17-8/Tritium; 61-90-5/Leucine; 9010-66-6/Zein

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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