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Essential function in chloroplast recognition of the ferredoxin transit peptide processing region

MGG Molecular & General Genetics, ISSN: 0026-8925, Vol: 216, Issue: 1, Page: 178-182
1989
  • 37
    Citations
  • 0
    Usage
  • 3
    Captures
  • 0
    Mentions
  • 0
    Social Media
Metric Options:   Counts1 Year3 Year

Metrics Details

  • Citations
    37
    • Citation Indexes
      37
  • Captures
    3

Article Description

Plant ferredoxin is a nuclear-encoded chloroplast protein that is synthesized in the cytoplasm as a transit peptide-containing precursor molecule. To identify functional regions in the pre-ferredoxin transit peptide we constructed mutants with deletions of increasing length from the processing site toward the amino-terminus of the precursor. The mutant proteins were tested in an in vitro chloroplast binding and import assay. Deletion of the amino acids adjacent to the processing site completely abolishes binding and import. This region contains a sequence motif that is conserved among different precursor species. By constructing and testing mutants in the amino-terminal region of the mature part of the precursor protein, we found that this region of the molecule can greatly influence the import reaction. © 1989 Springer-Verlag.

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