Analysis of Maize Brittle-1 Alleles and a Defective Suppressor-Mutator-Induced Mutable Allele

A mutant allele of the maize brittle-1 (bt1) locus, brittle-1-mutable (bt1-m), was shown genetically and molecularly to result from the insertion of a defective Suppressor-mutator (dSpm) transposable element. An Spm-hybridizing restriction enzyme fragment, which cosegregates with the bt1-m allele an...

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Bibliographic Details
Published in:The Plant cell 1991-12, Vol.3 (12), p.1337-1348
Main Authors: Sullivan, Thomas D., Strelow, Lisa I., Illingworth, Charles A., Phillips, Ronald L., Nelson, Oliver E.
Format: Article
Language:English
Subjects:
Alleles
Amino Acid Sequence
Amino acids
Base Sequence
Cloning, Molecular
Complementary DNA
Corn
DNA
DNA Transposable Elements
Endosperm
Genetic loci
Genomics
Membrane Proteins - genetics
Membrane Proteins - metabolism
Molecular Sequence Data
Phenotype
Plant Proteins - genetics
Plant Proteins - metabolism
RNA
Sequence Homology, Amino Acid
Suppression, Genetic
Transposons
Zea mays - genetics
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Summary:A mutant allele of the maize brittle-1 (bt1) locus, brittle-1-mutable (bt1-m), was shown genetically and molecularly to result from the insertion of a defective Suppressor-mutator (dSpm) transposable element. An Spm-hybridizing restriction enzyme fragment, which cosegregates with the bt1-m allele and is absent from wild-type revertants of bt1-m, was identified and cloned. Non-Spm portions of it were used as probes to identify wild-type (Bt1) cDNAs in an endosperm library. The 4.3-kb bt1-m genomic clone contains a 3.3-kb dSpm, which is inserted in an exon and is composed of Spm termini flanking non-Spm sequences. RNA gel blot analyses, using a cloned Bt1 cDNA probe, indicated that Bt1 mRNA is present in the endosperm of developing kernels and is absent from embryo or leaf tissues. Several transcripts are produced by bt1-m. The deduced translation product from a 1.7-kb Bt1 cDNA clone has an apparent plastid transit peptide at its amino terminus and sequence similarity to several mitochondrial inner-envelope translocator proteins, suggesting a possible role in amyloplast membrane transport.
ISSN:1040-4651
1532-298X
DOI:10.1105/tpc.3.12.1337