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Related Experiment Videos

Poly(3-hydroxyvalerate) depolymerase of Pseudomonas lemoignei.

U Schöber1, C Thiel, D Jendrossek

  • 1Institut für Mikrobiologie der Universität Stuttgart, 70550 Stuttgart, Germany.

Applied and Environmental Microbiology
|April 1, 2000
PubMed
Summary
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Pseudomonas lemoignei utilizes polyhydroxyalkanoates (PHA) via depolymerase genes. Researchers identified the true poly(3-hydroxyvalerate) (PHV) depolymerase gene, phaZ6, correcting previous assumptions about phaZ4.

Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • Pseudomonas lemoignei possesses multiple polyhydroxyalkanoate (PHA) depolymerase genes (phaZ1-phaZ5) for utilizing short-chain-length hydroxyalkanoates (PHA(SCL)).
  • Four genes (phaZ1, phaZ2, phaZ3, phaZ5) were identified as encoding poly(3-hydroxybutyrate) (PHB) depolymerases.
  • The gene phaZ4 was previously speculated to encode poly(3-hydroxyvalerate) (PHV) depolymerase.

Purpose of the Study:

  • To re-evaluate the function of the phaZ4 gene in Pseudomonas lemoignei.
  • To identify the correct gene responsible for PHV depolymerase activity.
  • To characterize the identified PHV depolymerase and its gene.

Main Methods:

  • Comparative analysis of amino acid sequences obtained by Edman degradation and endoproteinase GluC digestion with DNA-deduced sequences.

Related Experiment Videos

  • Immunological assays using antibodies specific to PHV depolymerase.
  • Enzyme activity assays using PHV and poly(3-hydroxybutyrate) (PHB) as substrates.
  • Genomic library screening in Escherichia coli to identify the PHV depolymerase gene.
  • Gene expression and protein purification from recombinant E. coli.
  • Amino acid analysis and domain comparison of the purified protein.

    • Main Results:

    • The phaZ4 gene was shown to encode another PHB depolymerase, not PHV depolymerase, based on sequence discrepancies, lack of immunological reaction, and low PHV activity.
    • The true PHV depolymerase gene, designated phaZ6, was identified through genomic screening.
    • The PhaZ6 protein exhibited immunological identity to wild-type PHV depolymerase and high specific activities on both PHB and PHV substrates.
    • PhaZ6 encodes a protein with a catalytic domain, a Thr-rich linker region, and a substrate-binding domain, showing homology to other PHA(SCL) depolymerases.
    • Codon usage analysis suggests phaZ6 may have been acquired through horizontal gene transfer.

    Conclusions:

    • The gene phaZ4 encodes a PHB depolymerase, and phaZ6 is the correct gene for PHV depolymerase in Pseudomonas lemoignei.
    • PhaZ6 represents the first reported PHA(SCL) depolymerase gene expressed during growth on PHV with high PHV depolymerase activity.
    • Structural analysis reveals conserved domains among PHA(SCL) depolymerases, suggesting domain exchange during evolution.