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 language | English |
|---|---|
| Pages (from-to) | 809-816 |
| Number of pages | 8 |
| Journal | Journal of Proteome Research |
| Volume | 7 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - Feb 1 2008 |
| Externally published | Yes |
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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 journal › Article
}
TY - JOUR
T1 - Proteome analysis of pitcher fluid of the carnivorous plant Nepenthes alata
AU - Hatano, Naoya
AU - Hamada, Tatsuro
PY - 2008/2/1
Y1 - 2008/2/1
N2 - 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.
AB - 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.
KW - Carnivorous plants
KW - De novo sequencing
KW - Nepenthes
KW - PR protein
KW - Proteome
UR - http://www.scopus.com/inward/record.url?scp=39749087658&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=39749087658&partnerID=8YFLogxK
U2 - 10.1021/pr700566d
DO - 10.1021/pr700566d
M3 - Article
C2 - 18183948
AN - SCOPUS:39749087658
VL - 7
SP - 809
EP - 816
JO - Journal of Proteome Research
JF - Journal of Proteome Research
SN - 1535-3893
IS - 2
ER -