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Two different dihydroorotate dehydrogenases in Lactococcus lactis

P S Andersen1, P J Jansen, K Hammer

  • 1Department of Microbiology, Technical University of Denmark, Lyngby.

Journal of Bacteriology
|July 1, 1994
PubMed
Summary

Lactococcus lactis possesses two distinct pyrD genes for dihydroorotate dehydrogenase. Disrupting both genes is necessary for pyrimidine auxotrophy, revealing pathway redundancy.

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Area of Science:

  • Biochemistry
  • Microbiology
  • Molecular Biology

Background:

  • The pyrimidine de novo biosynthesis pathway is essential for cell growth and has been studied in various organisms.
  • This pathway involves six key enzymatic steps.
  • Understanding this pathway in Lactococcus lactis is crucial for its industrial applications and genetic manipulation.

Purpose of the Study:

  • To characterize the pyrimidine biosynthesis pathway in Lactococcus lactis.
  • To isolate and analyze the pyrD genes encoding dihydroorotate dehydrogenase.
  • To investigate the functional redundancy of the identified pyrD genes.

Main Methods:

  • Isolation and sequencing of two pyrD genes (pyrDa and pyrDb) from Lactococcus lactis.
  • Sequence homology analysis comparing deduced amino acid sequences to known dihydroorotate dehydrogenases.
  • Enzyme characterization using different electron acceptors in crude extracts.
  • Construction of pyrD gene mutants (single and double) to assess pyrimidine auxotrophy.

Main Results:

  • Two distinct pyrD genes, pyrDa and pyrDb, were identified in Lactococcus lactis.
  • The deduced amino acid sequences showed homology to dihydroorotate dehydrogenases from Saccharomyces cerevisiae and Bacillus subtilis.
  • The two enzymes could be differentiated using various electron acceptors.
  • Only the double mutant lacking functional pyrDa and pyrDb exhibited pyrimidine auxotrophy.

Conclusions:

  • Lactococcus lactis possesses two functional dihydroorotate dehydrogenase enzymes encoded by separate pyrD genes.
  • These two enzymes exhibit distinct characteristics and can be differentiated.
  • The pyrimidine de novo biosynthesis pathway in Lactococcus lactis displays functional redundancy, as only the simultaneous absence of both pyrD genes leads to a requirement for external pyrimidines.

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