The b-32 protein from maize endosperm: characterization of genomic sequences encoding two alternative central domains

Plant Mol Biol. 1990 Jun;14(6):1031-40. doi: 10.1007/BF00019399.

Abstract

As derived from a cDNA clone, the structure of the b-32 protein of Zea mays, a putative regulatory factor of zein expression, has a central acidic region separated by two domains covered by secondary structure motifs. In this work, three b-32 genomic clones were selected from two genomic libraries obtained from the maize inbred lines W64A and A69Y. The nucleotide sequences of the complete coding region of each b-32 gene, as well as long stretches of their 5' and 3' flanking regions, were determined. Introns are not present in the b-32 genomic sequences. Minor variations among the three genes and an earlier reported b-32 cDNA indicates that they constitute a gene family showing a characteristic polymorphism. Such a polymorphism is highly evident in large segments of the upstream regulatory sequences. Interestingly, when compared with cDNA (W64A) or with gene b-32.120 (W64A), the genes b-32.129 (W64A) and b-32.152 (A69Y) show three jumps of the reading frame in the central part of the coding region, resulting in a completely different sequence of the b-32 protein central domain. In all cases, variations in the N- and C-terminal domains account only for microheterogeneity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Cloning, Molecular
  • DNA / genetics
  • Genes, Plant*
  • Molecular Sequence Data
  • Multigene Family
  • Plant Proteins / genetics*
  • Plants / genetics*
  • Polymorphism, Genetic
  • Zea mays / genetics

Substances

  • B-32 protein, Zea mays
  • Plant Proteins
  • DNA