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Related Experiment Videos

Identifying functional domains within terpene cyclases using a domain-swapping strategy

K Back1, J Chappell

  • 1Plant Physiology/Biochemistry/Molecular Biology Program, University of Kentucky, Lexington 40546-0091, USA.

Proceedings of the National Academy of Sciences of the United States of America
|June 25, 1996
PubMed
Summary

Cyclic terpene cyclases exhibit conserved gene structures, allowing for novel enzyme creation. Exon swapping between Nicotiana tabacum 5-epi-aristolochene synthase (TEAS) and Hyoscyamus muticus vetispiradiene synthase (HVS) genes generated chimeric enzymes with dual product specificities.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Plant Science

Background:

  • Cyclic terpenes and terpenoids are vital plant compounds with pharmaceutical applications.
  • Terpene cyclases (TCs) are key enzymes in synthesizing these compounds from allylic diphosphate substrates.
  • Comparative analysis of TCs reveals significant sequence and gene structure conservation.

Purpose of the Study:

  • To investigate the role of conserved exonic domains in terpene cyclase function and specificity.
  • To explore the potential for generating novel terpene cyclases through domain swapping.

Main Methods:

  • Molecular comparisons of terpene cyclase genes.
  • Exon swapping experiments between Nicotiana tabacum 5-epi-aristolochene synthase (TEAS) and Hyoscyamus muticus vetispiradiene synthase (HVS) genes.

Related Experiment Videos

  • Expression and characterization of chimeric enzymes in bacteria.

    • Main Results:

    • Specific exons (TEAS exon 4, HVS exon 6) conferred distinct product specificities.
    • Chimeric enzymes synthesized products characteristic of both parent enzymes.
    • Exon 5 influenced the product ratio in chimeric enzymes.

    Conclusions:

    • Catalytic activities are associated with conserved, separate exonic domains in terpene cyclases.
    • This modularity offers a general strategy for creating novel terpene cyclases with tailored functions.