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Characterization of a chloroplast sequence-specific DNA binding factor.

E Lam1, L Hanley-Bowdoin, N H Chua

  • 1Laboratory of Plant Molecular Biology, Rockefeller University, New York, New York 10021-6399.

The Journal of Biological Chemistry
|June 15, 1988
PubMed
Summary
This summary is machine-generated.

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Specific DNA binding factors in chloroplasts regulate gene expression. These factors bind to the intergenic region between rbcL and atpB genes, influencing transcription initiation.

Area of Science:

  • Chloroplast molecular biology
  • Plant gene regulation
  • Molecular genetics

Background:

  • The chloroplast genome encodes essential proteins like rbcL and atpB.
  • These genes are divergently transcribed, with an intergenic region between them.
  • Understanding regulatory elements in this region is key to chloroplast gene expression.

Purpose of the Study:

  • To identify and characterize DNA binding factors in the intergenic region of chloroplast genes.
  • To investigate the role of these factors in regulating chloroplast gene transcription.
  • To compare binding sites across different plant species.

Main Methods:

  • Exonuclease III digestion protection assays using chloroplast DNA probes.
  • Competition assays with intergenic DNA sequences.

Related Experiment Videos

  • Gel filtration chromatography to determine molecular weight.
  • Comparison of intergenic regions across maize, tobacco, spinach, and pea.

    • Main Results:

    • Specific DNA binding factors were identified in the intergenic region between rbcL and atpB genes.
    • The binding domain is conserved across multiple plant species.
    • A DNA-binding complex with a molecular weight of approximately 115,000 was detected.
    • Escherichia coli RNA polymerase demonstrated binding to promoter-like regions.

    Conclusions:

    • A novel chloroplast DNA binding factor plays a role in regulating gene expression.
    • The identified binding sites are conserved, suggesting functional importance.
    • Chloroplast promoters may interact with RNA polymerase similarly to prokaryotic systems.