Proteome analysis of pitcher fluid of the carnivorous plant Nepenthes alata

Naoya Hatano, Tatsuro Hamada

Research output: Contribution to journalArticle

67 Citations (Scopus)

Abstract

The genus Nepenthes comprises carnivorous plants that digest insects in pitcher fluid to supplement their nitrogen uptake. In a recent study, two acid proteinases (nepenthesins I and II) were purified from the pitcher fluid. However, no other enzymes involved in prey digestion have been identified, although several enzyme activities have been reported. To identify all the proteins involved, we performed a proteomic analysis of Nepenthes pitcher fluid. The secreted proteins in pitcher fluid were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and several protein bands were detected by silver staining. The proteins were identified by in-gel tryptic digestion, de novo peptide sequencing, and homology searches against public databases. The proteins included homologues of β-D-xylosidase, β-1,3-glucanase, chitinase, and thaumatin-like protein, most of which are designated "pathogenesis-related proteins". These proteins presumably inhibit bacterial growth in the pitcher fluid to ensure sufficient nutrients for Nepenthes growth.

Original languageEnglish
Pages (from-to)809-816
Number of pages8
JournalJournal of Proteome Research
Volume7
Issue number2
DOIs
Publication statusPublished - Feb 1 2008
Externally publishedYes

Fingerprint

Proteome
Fluids
Proteins
Digestion
Xylosidases
Chitinases
Silver Staining
Enzyme activity
Enzymes
Growth
Electrophoresis
Silver
Sodium Dodecyl Sulfate
Proteomics
Nutrients
Insects
Polyacrylamide Gel Electrophoresis
Nitrogen
Gels
Databases

Keywords

  • Carnivorous plants
  • De novo sequencing
  • Nepenthes
  • PR protein
  • Proteome

ASJC Scopus subject areas

  • Biochemistry
  • Biotechnology
  • Genetics

Cite this

Proteome analysis of pitcher fluid of the carnivorous plant Nepenthes alata. / Hatano, Naoya; Hamada, Tatsuro.

In: Journal of Proteome Research, Vol. 7, No. 2, 01.02.2008, p. 809-816.

Research output: Contribution to journalArticle

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