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

Plant Molecular Biology
H HartingsM Motto

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.

References

Dec 1, 1977·Proceedings of the National Academy of Sciences of the United States of America·F SangerA R Coulson
Nov 15, 1983·Journal of Molecular Biology·A M FrischaufN Murray
Jan 1, 1981·Annual Review of Biochemistry·R Breathnach, P Chambon

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Citations

Feb 1, 1994·Plant Molecular Biology·L PirovanoM Motto
May 1, 1991·Molecular & General Genetics : MGG·H HartingsM Motto
Oct 28, 1996·Molecular & General Genetics : MGG·J R MuthR D Thompson
Dec 21, 1993·Biochimica Et Biophysica Acta·L BarbieriF Stirpe
Jun 8, 2007·Plant Biotechnology Journal·Nancy M HoumardThomas M Malvar

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