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-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 GlcNAc2Man(3-5)Xyl. 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.
Daubenfeld
Thorsten
T
Laboratoire des Mécanismes Réactionnels, UMR 7651, Ecole Polytechnique, 91128 Palaiseau Cedex, France.
Hossann
Martin
M
Trommer
Wolfgang E
WE
Niedner-Schatteburg
Gereon
G
D000595:Amino Acid Sequence; D004591:Electrophoresis, Polyacrylamide Gel; D005583:Fourier Analysis; D006031:Glycosylation; D006868:Hydrolysis; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry*; D054789:Ribosome Inactivating Proteins, Type 1; D017386:Sequence Homology, Amino Acid
D010940:Plant Proteins; D054789:Ribosome Inactivating Proteins, Type 1; C025674:GEL protein, Gelonium multiflorum