Reference "Nucleotide sequence analysis of alpha-amylase and thiol protease genes that are hormonally regulated in barley aleurone cells"

Reference ID

8827

Title

Nucleotide sequence analysis of alpha-amylase and thiol protease genes that are hormonally regulated in barley aleurone cells

Source

Nucleic acids research, 1987, vol. 15, pp. 2515-2535

Authors (3)

Whittier-R-F	Dean-D-A
Rogers-J-C

Abstract

We have determined the nucleotide sequences of Amy32b, a type A alpha-amylase
gene, and of the gene for aleurain, a thiol protease closely related to
mammalian cathepsin H. Both are expressed in barley aleurone cells under
control of the plant hormones gibberellic acid and abscisic acid, but only
aleurain is expressed at high levels in other barley tissues. Sequence analysis
indicates that the 5' end of the aleurain gene, comprising 3 exons and 2
introns, may have become associated with the remainder of the gene, encoding
the protease domain of the protein, by some sort of recombination event. This
5' domain of the gene is very G + C-rich and is flanked by inverted repetitive
sequences. We found two different groups of homologous sequence elements. The
first group consists of four blocks of sequences conserved in the same spatial
arrangement in both genes; these are arranged at similar intervals upstream
from the Amy32b TATA box and from a TATA box present in intron 3 of aleurain,
outside of the 5' domain and upstream from the protease domain. A part of two
of these conserved sequences is similar to the core sequence of certain
enhancer elements characterized from mammalian cells. The second group of
homologous elements is present in the upstream region of both genes. We
speculate that these conserved sets of sequences may have some role in either
the tissue specificity of expression of the genes or in some part of the
hormonal regulation imposed on them.