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Related Experiment Videos

Identification and proteolytic processing of procardosin A

M Ramalho-Santos1, P Veríssimo, L Cortes

  • 1Departamento de Bioquímica and the Centro de Neurociências e Biologia Celular, Universidade de Coimbra, Portugal.

European Journal of Biochemistry
|August 6, 1998
PubMed
Summary

Plant aspartic proteinases feature a unique insert (PSI) with unknown function. This study reveals PSI is removed early during cardosin A processing, before the prosegment, suggesting a role in enzyme maturation.

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Area of Science:

  • Biochemistry
  • Plant Molecular Biology

Background:

  • Plant aspartic proteinases possess a plant-specific insert (PSI) of unknown function.
  • PSI shows similarity to animal saposins but lacks similarity to other aspartic proteinases.
  • PSI's elusive nature at the protein level suggests it is removed during processing.

Purpose of the Study:

  • To investigate the proteolytic processing of cardosin A, a major plant aspartic proteinase.
  • To understand the molecular relevance and processing of the plant-specific insert (PSI).

Main Methods:

  • Identification of procardosin A using immunoblotting with specific antibodies.
  • Analysis of procardosin A processing during flower maturation.
  • In vitro processing studies at different pH values and with inhibitors.

Related Experiment Videos

  • Sequence analysis to identify cleavage sites.

    • Main Results:

    • Procardosin A, the precursor containing PSI, was identified.
    • PSI is removed proteolytically before the prosegment during maturation.
    • PSI removal occurs at acidic pH (3.0) and is inhibited by pepstatin A.
    • Cleavage is conformation-dependent, requiring the precursor form.

    Conclusions:

    • A model for cardosin A proteolytic processing is proposed, with PSI removed early.
    • PSI removal likely occurs via an aspartic proteinase.
    • The findings shed light on the molecular and physiological significance of PSI in plant aspartic proteinases.