Back to Search
Start Over
The Maize Floury1 Gene Encodes a Novel Endoplasmic Reticulum Protein Involved in Zein Protein Body Formation
- Source :
- The Plant Cell. 19:2569-2582
- Publication Year :
- 2007
- Publisher :
- Oxford University Press (OUP), 2007.
-
Abstract
- The maize (Zea mays) floury1 (fl1) mutant was first reported almost 100 years ago, but its molecular identity has remained unknown. We report the cloning of Fl1, which encodes a novel zein protein body membrane protein with three predicted transmembrane domains and a C-terminal plant-specific domain of unknown function (DUF593). In wild-type endosperm, the FL1 protein accumulates at a high level during the period of zein synthesis and protein body development and declines to a low level at kernel maturity. Immunogold labeling showed that FL1 resides in the endoplasmic reticulum surrounding the protein body. Zein protein bodies in fl1 mutants are of normal size, shape, and abundance. However, mutant protein bodies ectopically accumulate 22-kD α-zeins in the γ-zein–rich periphery and center of the core, rather than their normal discrete location in a ring at outer edge of the core. The 19-kD α-zein is uniformly distributed throughout the core in wild-type protein bodies, and this distribution is unaffected in fl1 mutants. Pairwise yeast two-hybrid experiments showed that FL1 DUF593 interacts with the 22-kD α-zein. Results of these studies suggest that FL1 participates in protein body formation by facilitating the localization of 22-kD α-zein and that this is essential for the formation of vitreous endosperm.
- Subjects :
- Protein Folding
Vesicle-associated membrane protein 8
Zein
Molecular Sequence Data
Plant Science
Biology
Endoplasmic Reticulum
Zea mays
HSPA4
Gene Expression Regulation, Plant
Mutant protein
Two-Hybrid System Techniques
HSPA2
Amino Acid Sequence
RNA, Messenger
Alleles
Conserved Sequence
Phylogeny
Research Articles
Plant Proteins
Endoplasmic reticulum
Membrane Proteins
food and beverages
STIM1
Intracellular Membranes
Cell Biology
Protein Structure, Tertiary
Molecular Weight
Protein Transport
Transmembrane domain
Phenotype
Biochemistry
Protein body
Mutation
Seeds
Protein Binding
Subjects
Details
- ISSN :
- 1532298X
- Volume :
- 19
- Database :
- OpenAIRE
- Journal :
- The Plant Cell
- Accession number :
- edsair.doi.dedup.....76317d1423f8eb31c18b6992e7e88049
- Full Text :
- https://doi.org/10.1105/tpc.107.053538