Plastid targeting of E. coli β-glucuronidase and ADP-glucose pyrophosphorylase in maize (Zea mays L.) cells

Douglas A. Russell, David L. DeBoer, David M. Stark, Jack Preiss, Michael E. Fromm

Research output: Contribution to journalArticle

12 Scopus citations

Abstract

Dicot and monocot chloroplast targeting peptides (CTPs) were evaluated for their effect on targeting, processing, and expression of two reporter proteins in maize cells. When tested transiently in maize leaf protoplasts, the maize ribulose bisphosphate carboxylase small subunit CTP required the inclusion of the amino terminus of mature small subunit protein to target β-glucuronidase (GUS) to the plastid. To remove this amino terminal extension from GUS after import and processing, a repeat of the native processing site was inserted between the native mature protein and the reporter protein. This repeat processing site was used with less efficiency than the native site. Parallel constructs using the Arabidopsis thaliana small subunit and maize granule-bound starch synthase CTPs also localized GUS, but varied in repeat site use and GUS expression levels. Data from the CTP fusions with GUS were generally confirmed with fusions to an allosteric variant of E. coli ADP-glucose pyrophosphorylase. Plastid targeting of this enzyme was required for starch enhancement of transgenic BMS cells.

Original languageEnglish (US)
Pages (from-to)24-27
Number of pages4
JournalPlant Cell Reports
Volume13
Issue number1
DOIs
StatePublished - Nov 1 1993

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ASJC Scopus subject areas

  • Agronomy and Crop Science
  • Plant Science

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