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. 1987 Feb;6(2):287–294. doi: 10.1002/j.1460-2075.1987.tb04752.x

Influence of transposable elements on the structure and function of the A1 gene of Zea mays

Zsuzsanna Schwarz-Sommer 1, Nancy Shepherd 1, Eckhard Tacke 1, Alfons Gierl 1, Wolfgang Rohde 1, Lise Leclercq 1, Maryann Mattes 1, Rita Berndtgen 1, Peter A Peterson 2, Heinz Saedler 1
PMCID: PMC553393  PMID: 15981326

Abstract

The structure of the A1 gene of Zea mays was determined by sequencing cDNA and genomic clones. The gene is composed of four exons and three short introns. The 40.1-kd A1 protein is an NADPH-dependent reductase. Germinal derivatives of the mutable a1-ml allele with either recessive or wild-type phenotype have been isolated. Sequence analysis of these revertant alleles indicates that frame-shift mutations abolish A1 gene function, whereas one additional amino acid within the protein sequence still allows wild-type gene expression. The presence of a second, promoter-like structure, upstream of the functional A1 gene promoter is discussed with respect to its possible involvement in differential expression of the A1 gene. The structure of the a1-m2 8004, 3456 and 4412 alleles, featuring distinguishable phenotypes in the presence of Spm(En), was also determined. In all alleles the 1080-bp-long inhibitor (I) element is located 15 bp upstream of the CAAT box of the A1 gene promoter. The unusual response of al-m2 alleles to trans-active signals of the Spm(En) element is discussed with respect to the position of the I inserts. Also presented are data on the structure and insertion sites of transposable elements determined by cloning and sequencing of the mutable a1 alleles a1-mpapu, a1-mr 102 and al-ml.

Keywords: NADPH-dependent reductase, insertion mutation, excision, Spm co-expression, altered promoter

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