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THE PLANT CELL, Vol 1, Issue 3 313-328, Copyright © 1989 by American Society of Plant Biologists
Characterization of the Glycinin Gene Family in Soybean
N. C. Nielsen, C. D. Dickinson, T. J. Cho, V. H. Thanh, B. J. Scallon, R. L. Fischer, T. L. Sims, G. N. Drews and R. B. Goldberg
U.S. Department of Agriculture/Agricultural Research Service, Department of Agronomy, Purdue University, West Lafayette, Indiana 47907
We characterized the structure, organization, and expression of genes that
encode the soybean glycinins, a family of storage proteins synthesized
exclusively in seeds during embryogenesis. Five genes encode the
predominant glycinin subunits found in soybeans, and they have each been
cloned, sequenced, and compared. The five genes have diverged into two
subfamilies that are designated as Group-I and Group-II glycinin genes.
Each glycinin gene contains four exons and three introns like genes that
encode related proteins in other legumes. Two other genes have been
identified and designated as "glycinin-related" because they hybridize
weakly with the five glycinin genes. Although not yet characterized,
glycinin-related genes could encode other glycinin subunit families whose
members accumulate in minor amounts in seeds. The three Group-I glycinin
genes are organized into two chromosomal domains, each about 45 kilobase
pairs in length. The two domains have a high degree of homoeology, and
contain at least five genes each that are expressed either in embryos or in
mature plant leaves. Gel blot studies with embryo mRNA, as well as
transcription studies with 32P-RNA synthesized in vitro from purified
embryo nuclei, indicate that glycinin and glycinin-related genes become
transcriptionally activated in a coordinated fashion early in
embryogenesis, and are repressed coordinately late in seed development. In
addition to transcriptional control processes, posttranscriptional events
also are involved in regulating glycinin and glycinin-related mRNA levels
during embryogenesis.
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