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Related Experiment Videos

Screening for beta-poly(L-malate) binding proteins by affinity chromatography.

Thomas Göttler1, Eggehard Holler

  • 1Institut für Biophysik und Physikalische Biochemie, Universität Regensburg, D-93040 Regensburg, Germany.

Biochemical and Biophysical Research Communications
|February 16, 2006
PubMed
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Poly(beta-L-malic acid), a slime mold polymer, binds to proteins involved in cell mobility. Researchers identified these proteins using affinity chromatography, revealing a large complex protein in Physarum polycephalum.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Poly(beta-L-malic acid) is a unique polymer found in myxomycetes (slime molds).
  • It plays a role in organizing protein mobility within the giant multinucleated plasmodia of these organisms.

Purpose of the Study:

  • To identify proteins that bind to poly(beta-L-malic acid) in Physarum polycephalum.
  • To characterize the properties and cellular localization of these poly(beta-L-malic acid)-binding proteins.

Main Methods:

  • Affinity chromatography using 1,6-diamino-n-hexane-Sepharose-coupled poly(malic acid).
  • Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and non-denaturing PAGE for molecular mass and complex analysis.
  • Western blotting and silver staining for protein detection.

Related Experiment Videos

  • 2-dimensional non-denaturing PAGE/SDS-PAGE for complex/subunit analysis.
  • Gel shift assays to assess DNA binding.

    • Main Results:

    • Identification of poly(malate)-binding proteins in cellular extracts of Physarum polycephalum.
    • A significant 370 kDa protein complex was found, dissociating into 11 subunits (11-29 kDa).
    • Poly(malate)-binding proteins were most abundant in nuclei, followed by cytoplasm and membranes.
    • Proteins demonstrated binding to nucleic acids in gel shift experiments.
    • Poly(malate) is proposed as a functional equivalent to eukaryotic aspartate repeats.

    Conclusions:

    • Poly(beta-L-malic acid) interacts with specific proteins, particularly within the nucleus.
    • These proteins are complex and exhibit nucleic acid binding properties.
    • Poly(malic acid) may serve a structural or functional role analogous to aspartate repeats in eukaryotes.