C-terminal post-translational proteolysis of plant lectins and their recombinant forms expressed in Escherichia coli. Characterization of "ragged ends" by mass spectrometry

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DOIResolve DOI: http://doi.org/10.1074/jbc.270.6.2563
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TypeArticle
Journal titleJournal of Biological Chemistry
ISSN0021-9258
Volume270
Issue6
Pages25632570; # of pages: 8
AbstractElectrospray mass spectrometry was used to accurately measure the molecular masses of single chain lectins from legume seeds and also of three recombinant lectins, expressed in Escherichia coli. The five single chain lectins, Erythrina corallodendron lectin, soybean and peanut agglutinins, Dolichos biflorus lectin, and Phaseolus vulgaris hemagglutinin E, all showed evidence of C-terminal proteolytic processing, in some cases to “ragged” ends, when their masses were compared to those expected from their cDNA sequences and their known carbohydrate chains. Recombinant forms of the lectins from E. corallodendron, soybean, and peanut also showed C-terminal trimming, but not to the same points as the natural forms. Discrepancies between the protein and cDNA sequences of the E. corallodendron lectin were resolved by combined liquid chromatography-mass spectrometry peptide mapping and protein sequencing experiments, and the presence of a second glycosylation site was demonstrated. Our data show that all of these lectins undergo C-terminal proteolytic processing of a readily attacked peptide segment. This trimming is frequently imprecise, and the resulting heterogeneity may be a major contributor to the appearance of isolectin forms of these proteins.
Publication date
LanguageEnglish
AffiliationNRC Institute for Biological Sciences; NRC Institute for Marine Biosciences; National Research Council Canada
Peer reviewedNo
NRC numberYOUNG1995A
NPARC number9377473
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Record identifier4a95ff4d-df57-4d74-a78c-51a8181d86ec
Record created2009-07-10
Record modified2016-05-09
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