A defective signal peptide in the maize high-lysine mutant floury 2

The maize floury 2 (fl2) mutation enhances the lysine content of the grain, but the soft texture of the endosperm makes it unsuitable for commercial production. The mutant phenotype is linked with the appearance of a 24-kDa alpha-zein protein and increased synthesis of binding protein, both of which...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1995-07, Vol.92 (15), p.6828-6831
Main Authors: Coleman, C.E. (University of Arizona, Tucson, AZ.), Lopes, M.A, Gillikin, J.W, Boston, R.S, Larkins, B.A
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino acids
Base Sequence
Blotting, Southern
Botany
Cloning, Molecular
COMPOSICION QUIMICA
COMPOSITION CHIMIQUE
Corn
DNA
Electrophoresis, Gel, Two-Dimensional
Endosperm
Gels
GENE
GENES
Genetic Linkage
Genetic mutation
Genomics
Lysine - analysis
Molecular Sequence Data
MUTACION
MUTANT
MUTANTES
MUTATION
Plant cells
Polymorphism, Restriction Fragment Length
PROLAMINAS
PROLAMINE
Protein Precursors - genetics
Protein Processing, Post-Translational
Protein Sorting Signals - genetics
Proteins
SECUENCIA NUCLEICA
Seeds - chemistry
Seeds - genetics
Sequence Analysis
Sequence Homology, Amino Acid
SEQUENCE NUCLEIQUE
ZEA MAYS
Zea mays - chemistry
Zea mays - genetics
Zein - chemistry
Zein - genetics
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Description
Summary:The maize floury 2 (fl2) mutation enhances the lysine content of the grain, but the soft texture of the endosperm makes it unsuitable for commercial production. The mutant phenotype is linked with the appearance of a 24-kDa alpha-zein protein and increased synthesis of binding protein, both of which are associated with irregularly shaped protein bodies. We have cloned the gene encoding the 24-kDa protein and show that it is expressed as a 22-kDa alpha-zein with an uncleaved signal peptide. Comparison of the deduced N-terminal amino acid sequence of the 24-kDa alpha-zein protein with other alpha-zeins revealed an alanine to valine substitution at the C-terminal position of the signal peptide, a histidine insertion within the seventh alpha-helical repeat, and an alanine to threonine substitution with the same alpha-helical repeat of the protein. Structural defects associated with this alpha-zein explain many of the phenotypic effects of the fl2 mutation
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.92.15.6828