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Control of Maize Zein Gene Expression

  • Rebecca S. Boston
  • Brian A. Larkins
Part of the Genetic Engineering book series (GEPM)

Abstract

Seed storage proteins provide useful model systems for the study of gene regulation. These proteins are found only in the seed and in most angiosperms account for approximately half of the total seed protein. The storage proteins in maize seed are a group of prolamin proteins called zeins. Zeins are synthesized in the developing endosperm by membrane-bound polyribosomes and associate into insoluble aggregates called “protein bodies” within the lumen of the rough endoplasmic reticulum (1). Zein proteins are isolated from either mature seed or protein bodies of developing seeds by extraction with alcoholic solutions (70% ethanol or 55% isopropanol) in the presence of reducing agents such as 2-mercaptoethanol. Extraction with 70% alcohol alone results in recovery of proteins of 22 and 19 kD while extraction with alcohol plus 2-mercaptoethanol yields proteins of 27, 22, 19, 15, 14, and 10 kD (2). When separated by 2-dimensional gel electrophoresis, the 22 and 19 kD components each resolve into a number of charged isomers, but the proteins of 27, 15, 14, and 10 kD migrate as single polypeptides. Based on immunocytochemical analysis, the 22 and 19 kD proteins are distributed throughout the matrix of the protein body, whereas the 27, 15, and 14 kD proteins are localized near its surface (C. Lending, A. L. Kriz, C. Bracker and B. A. Larkins, unpublished data).

Keywords

Seed Storage Protein Chloramphenicol Acetyl Transferase Zein Protein Chloramphenicol Acetyl Transferase Activity Zein Gene 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1987

Authors and Affiliations

  • Rebecca S. Boston
    • 1
  • Brian A. Larkins
    • 1
  1. 1.Department of Botany and Plant PathologyPurdue UniversityWest LafayetteUSA

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