Document Detail


Identification of the protein storage vacuole and protein targeting to the vacuole in leaf cells of three plant species.
MedLine Citation:
PMID:  14730078     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Protein storage vacuoles (PSVs) are specialized vacuoles devoted to the accumulation of large amounts of protein in the storage tissues of plants. In this study, we investigated the presence of the storage vacuole and protein trafficking to the compartment in cells of tobacco (Nicotiana tabacum), common bean (Phaseolus vulgaris), and Arabidopsis leaf tissue. When we expressed phaseolin, the major storage protein of common bean, or an epitope-tagged version of alpha-tonoplast intrinsic protein (alpha-TIP, a tonoplast aquaporin of PSV), in protoplasts derived from leaf tissues, these proteins were targeted to a compartment ranging in size from 2 to 5 microm in all three plant species. Most Arabidopsis leaf cells have one of these organelles. In contrast, from one to five these organelles occurred in bean and tobacco leaf cells. Also, endogenous alpha-TIP is localized in a similar compartment in untransformed leaf cells of common bean and is colocalized with transiently expressed epitope-tagged alpha-TIP. In Arabidopsis, phaseolin contained N-glycans modified by Golgi enzymes and its traffic was sensitive to brefeldin A. However, trafficking of alpha-TIP was insensitive to brefeldin A treatment and was not affected by the dominant-negative mutant of AtRab1. In addition, a modified alpha-TIP with an insertion of an N-glycosylation site has the endoplasmic reticulum-type glycans. Finally, the early step of phaseolin traffic, from the endoplasmic reticulum to the Golgi complex, required the activity of the small GTPase Sar1p, a key component of coat protein complex II-coated vesicles, independent of the presence of the vacuolar sorting signal in phaseolin. Based on these results, we propose that the proteins we analyzed are targeted to the PSV or equivalent organelle in leaf cells and that proteins can be transported to the PSV by two different pathways, the Golgi-dependent and Golgi-independent pathways, depending on the individual cargo proteins.
Authors:
Misoon Park; Soo Jin Kim; Alessandro Vitale; Inhwan Hwang
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2004-01-15
Journal Detail:
Title:  Plant physiology     Volume:  134     ISSN:  0032-0889     ISO Abbreviation:  Plant Physiol.     Publication Date:  2004 Feb 
Date Detail:
Created Date:  2004-02-17     Completed Date:  2004-06-10     Revised Date:  2010-09-21    
Medline Journal Info:
Nlm Unique ID:  0401224     Medline TA:  Plant Physiol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  625-39     Citation Subset:  IM    
Affiliation:
Center for Plant Intracellular Trafficking, Pohang University of Science and Technology, Pohang, 790-784, Korea.
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MeSH Terms
Descriptor/Qualifier:
Arabidopsis / genetics,  metabolism
Arabidopsis Proteins / genetics,  metabolism
Brefeldin A / pharmacology
Gene Expression Regulation, Plant
Golgi Apparatus / metabolism
Immunohistochemistry
Membrane Proteins / genetics,  metabolism*
Mutation
Phaseolus / genetics,  metabolism
Plant Leaves / cytology,  genetics,  metabolism*
Plant Proteins / genetics,  metabolism*
Plants / genetics,  metabolism*
Protein Transport / drug effects
Tobacco / genetics,  metabolism
Vacuoles / metabolism*
rab GTP-Binding Proteins / genetics,  metabolism
Chemical
Reg. No./Substance:
0/ATRAB ALPHA protein, Arabidopsis; 0/Arabidopsis Proteins; 0/Membrane Proteins; 0/Plant Proteins; 104042-75-3/phaseolin protein, Phaseolus vulgaris; 130960-59-7/alpha-TIP protein, Phaseolus vulgaris; 20350-15-6/Brefeldin A; EC 3.6.1.-/rab GTP-Binding Proteins
Comments/Corrections

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


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