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Related Experiment Videos

Higher plants possess two structurally different poly(ADP-ribose) polymerases

E Babiychuk1, P B Cottrill, S Storozhenko

  • 1Departement Genetica, Vlaams Interuniversitair Instituut voor Biotechnologie (VIB), Universiteit Gent, Belgium.

The Plant Journal : for Cell and Molecular Biology
|October 21, 1998
PubMed
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Plant poly(ADP-ribose) polymerase (PARP) biology is complex. Researchers identified two plant PARP types, including non-classical APP proteins, and confirmed APP nuclear localization and DNA-dependent activity.

Area of Science:

  • Plant molecular biology
  • Enzymology
  • Cellular stress response

Background:

  • Poly(ADP-ribose) polymerase (PARP) is crucial in mammalian stress response via poly(ADP-ribose) synthesis.
  • Plant PARP biology is less understood, with diverse homologues potentially existing beyond classical types.
  • Two plant PARP families identified: classical Zn-finger-containing (ZAP) and non-classical (APP, NAP) lacking this domain.

Purpose of the Study:

  • To investigate the function and localization of plant non-classical PARP proteins, specifically APP.
  • To confirm the enzymatic activity and cellular location of recombinant APP.
  • To analyze the transcriptional regulation of the app gene in response to cellular stress.

Main Methods:

  • Enzymatic assays using recombinant APP protein.

Related Experiment Videos

  • Cytological experiments to determine protein localization in yeast.
  • Analysis of transgenic tobacco plants expressing an APP-beta-glucuronidase fusion.
  • Promoter activity assays in cells with DNA ligase I deficiency.

    • Main Results:

    • Recombinant APP protein demonstrated DNA-dependent poly(ADP-ribose) polymerase activity in yeast.
    • APP was localized to the nucleus in yeast cells.
    • Nuclear localization of APP was confirmed in transgenic tobacco plants.
    • The app promoter was transcriptionally upregulated in cells undergoing programmed cell death due to DNA ligase I deficiency.

    Conclusions:

    • Plant non-classical PARP proteins, like APP, possess DNA-dependent enzymatic activity and are nuclear-localized.
    • APP plays a role in cellular processes, potentially related to DNA repair or stress response, as indicated by promoter upregulation.
    • Plant PARP biology is more diverse than previously assumed, involving non-classical members with distinct functions.