On the contentious sequence and glycosylation motif of the ribosome inactivating plant protein gelonin

The amino acid sequence and the glycosylation motif of the ribosome inactivating protein (RIP) gelonin are identified by Fourier transform ion cyclotron resonance mass spectrometry. Intact gelonin as isolated from the seeds of Gelonium multiflorum consists of at least three different post-translatio...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2005-08, Vol.333 (3), p.984-989
Main Authors: Daubenfeld, Thorsten, Hossann, Martin, Trommer, Wolfgang E., Niedner-Schatteburg, Gereon
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Chemical Sciences
Electrophoresis, Polyacrylamide Gel
Fourier Analysis
FT-ICR mass spectrometry
Gelonin
Gelonium multiflorum
Glycosylation
Hydrolysis
Immunoconjugates
Mass Spectrometry
Molecular Sequence Data
or physical chemistry
Plant Proteins - chemistry
Post-translational modification
Ribosome Inactivating Proteins, Type 1
Sequence Homology, Amino Acid
Theoretical and
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Summary:The amino acid sequence and the glycosylation motif of the ribosome inactivating protein (RIP) gelonin are identified by Fourier transform ion cyclotron resonance mass spectrometry. Intact gelonin as isolated from the seeds of Gelonium multiflorum consists of at least three different post-translational modified forms: analysis of gelonin peptides as obtained by proteolytic digestion is consistent with the amino acid sequence published by Nolan et al. High resolution mass determination established a glycosylation pattern of GlcNAc 2Man 3–5Xyl. N189 was identified as glycosylation site. The proposed glycan structure is consistent with a standard plant N-glycosylation pattern as found in other RIP. Based on these results we suggest that gelonin is located in the vacuole of Gelonium multiflorum seeds.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2005.06.008