On the contentious sequence and glycosylation motif of the ribosome inactivating plant protein gelonin - Archive ouverte HAL Access content directly
Journal Articles Biochemical and Biophysical Research Communications Year : 2005

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

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Abstract

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 GlcNAc2Man3-5Xyl. 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. © 2005 Elsevier Inc. All rights reserved.

Dates and versions

hal-00904634 , version 1 (08-12-2013)

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T. Daubenfeld, M. Hossann, W.E. Trommer, G. Niedner-Schatteburg. On the contentious sequence and glycosylation motif of the ribosome inactivating plant protein gelonin. Biochemical and Biophysical Research Communications, 2005, 333 (3), pp.984-989. ⟨10.1016/j.bbrc.2005.06.008⟩. ⟨hal-00904634⟩
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