Post-translational proteolytic processing and the isolectins of lentil and other Viciae seed lectins.
Electrospray mass spectrometry was used to identify precisely the proteolytic cleavage points within, and at the C-termini of, the proprotein forms of four Viciae lectins that give rise to their two-chain forms. The lectins examined were the pea and lentil lectins, favin and the Lathyrus odoratus lectin, which represent each of the four genera in this tribe. The molecular mass data showed single beta-chain forms for each lectin, with masses consistent with the available sequence and glycopeptide data, indicating that each came from a single proprotein. In contrast, the pea, lentil and L. odoratus alpha-chains occurred in as many as five forms, due to multiple C-terminal cleavage points. Only favin showed a single alpha-chain form. The alpha-chain mass data were again consistent with the sequence information available, except for the lentil lectin alpha-chain which was re-determined by protein sequencing. The two isolectin forms of this protein were shown to arise from alpha-chain species with and without residue Lys53. The mass spectrum of concanavalin A was also examined and both the single-chain form and the two fragment forms showed no evidence of C-terminal heterogeneity.
Young
N M
NM
Institute for Biological Sciences, National Research Council of Canada, Ottawa, Canada.
Watson
D C
DC
Thibault
P
P
D000595:Amino Acid Sequence; D007887:Fabaceae / Q000378:metabolism*; D037102:Lectins / Q000737:chemistry / Q000378:metabolism*; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D037121:Plant Lectins; D010946:Plants, Medicinal; D011499:Protein Processing, Post-Translational; D012639:Seeds / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid
D037102:Lectins; D037121:Plant Lectins