NDLI: Zein protein interactions, rather than the asymmetric distribution of zein mRNAs on endoplasmic reticulum membranes, influence protein body formation in maize endosperm.

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Zein protein interactions, rather than the asymmetric distribution of zein mRNAs on endoplasmic reticulum membranes, influence protein body formation in maize endosperm.

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Zein protein interactions, rather than the asymmetric distribution of zein mRNAs on endoplasmic reticulum membranes, influence protein body formation in maize endosperm.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Kim, Cheol Soo Woo Ym, Young-min Clore, Amy M. Burnett, Ronald J. Carneiro, Newton P. Larkins, Brian A.
Description	Country affiliation: United States Author Affiliation: Kim CS ( Department of Plant Sciences, University of Arizona, Tucson, Arizona 85721, USA.)
Abstract	Prolamin-containing protein bodies in maize endosperm are composed of four different polypeptides, the alpha-, beta-, gamma-, and delta-zeins. The spatial organization of zeins within the protein body, as well as interactions between them, suggests that the localized synthesis of gamma-zeins could initiate and target protein body formation at specific regions of the rough endoplasmic reticulum. To investigate this possibility, we analyzed the distribution of mRNAs encoding the 22-kD alpha-zein and the 27-kD gamma-zein proteins on cisternal and protein body rough endoplasmic reticulum membranes. In situ hybridization revealed similar frequencies of the mRNAs in both regions of the endoplasmic reticulum, indicating that the transcripts are distributed more or less randomly. This finding implies that zein protein interactions determine protein body assembly. To address this question, we expressed cDNAs encoding alpha-, beta-, gamma-, and delta-zeins in the yeast two-hybrid system. We found strong interactions among the 50-, 27-, and 16-kD gamma-zeins and the 15-kD beta-zein, consistent with their colocalization in developing protein bodies. Interactions between the 19- and 22-kD alpha-zeins were relatively weak, although each of them interacted strongly with the 10-kD delta-zein. Strong interactions were detected between the alpha- and delta-zeins and the 16-kD gamma-zein and the 15-kD beta-zein; however, the 50- and 27-kD gamma-zeins did not interact with the alpha- and delta-zein proteins. We identified domains within the 22-kD alpha-zein that bound preferentially the alpha- and delta-zeins and the beta- and gamma-zeins. Affinities between zeins generally were consistent with results from immunolocalization experiments, suggesting an important role for the 16-kD gamma-zein and the 15-kD beta-zein in the binding and assembly of alpha-zeins within the protein body.
File Format	HTM / HTML
ISSN	10404651
e-ISSN	1531298X
Journal	THE PLANT CELL ONLINE
Issue Number	3
Volume Number	14
Language	English
Publisher	American Society of Plant Biologists
Publisher Date	2002-03-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Discipline Botany Endoplasmic Reticulum Metabolism Rna, Messenger Genetics Zea Mays Zein Binding Sites Ultrastructure Immunoblotting In Situ Hybridization Protein Binding Protein Interaction Mapping Two-hybrid System Techniques Yeasts Research Support, U.s. Gov't, Non-p.h.s.
Content Type	Text
Resource Type	Article
Subject	Cell Biology Plant Science

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